1796:, also called DNAzymes or catalytic DNA, are artificial DNA-based catalysts that were first produced in 1994. Almost all DNAzymes require metal ions. Although ribozymes mostly catalyze cleavage of RNA substrates, a variety of reactions can be catalyzed by DNAzymes including RNA/DNA cleavage, RNA/DNA ligation, amino acid phosphorylation and dephosphorylation, and carbon–carbon bond formation. Yet, DNAzymes that catalyze RNA cleavage reaction are the most extensively explored ones. 10-23 DNAzyme, discovered in 1997, is one of the most studied catalytic DNAs with clinical applications as a therapeutic agent. Several metal-specific DNAzymes have been reported including the GR-5 DNAzyme (
982:
1338:
745:
1737:
1926:
1590:
33:
683:
1826:
1761:
in the early 1980s, ribozymes have been shown to be a distinct class of metalloenzymes. Many ribozymes require metal ions in their active sites for chemical catalysis; hence they are called metalloenzymes. Additionally, metal ions are essential for structural stabilization of ribozymes.
2845:
Kitajima N, Fujisawa K, Fujimoto C, Morooka Y, Hashimoto S, Kitagawa T, Toriumi K, Tatsumi K, Nakamura A (1992). "A new model for dioxygen binding in hemocyanin. Synthesis, characterization, and molecular structure of the
1960:
that these proteins bind to. Instead, the cofactor is essential for the stability of the tightly folded protein chain. In these proteins, the zinc ion is usually coordinated by pairs of cysteine and histidine side-chains.
1671:. In the process chlorophyll is oxidized. Later in the photosynthetic cycle, chlorophyll is reduced back again. This reduction ultimately draws electrons from water, yielding molecular oxygen as a final oxidation product.
95:
proteins, or infectious diseases. The abundance of metal binding proteins may be inherent to the amino acids that proteins use, as even artificial proteins without evolutionary history will readily bind metals.
1685:
Hydrogenases are subclassified into three different types based on the active site metal content: iron–iron hydrogenase, nickel–iron hydrogenase, and iron hydrogenase. All hydrogenases catalyze reversible
1878:
The protein has two approximately symmetrical domains, separated by a flexible "hinge" region. Binding of calcium causes a conformational change to occur in the protein. Calmodulin participates in an
1317:
cluster that is able to bind the dinitrogen molecule and, presumably, enable the reduction process to begin. The electrons are transported by the associated "P" cluster, which contains two
1465:
to near the diffusion-limited rate. The key to the action of these enzymes is a metal ion with variable oxidation state that can act either as an oxidizing agent or as a reducing agent.
83:. In another estimate, about one quarter to one third of all proteins are proposed to require metals to carry out their functions. Thus, metalloproteins have many different functions in
4171:
Jeoung JH, Fesseler J, Goetzl S, Dobbek H (2014). "Carbon
Monoxide. Toxic Gas and Fuel for Anaerobes and Aerobes: Carbon Monoxide Dehydrogenases". In Kroneck PM, Sosa Torres ME (eds.).
924:-carrying protein in the blood. Ceruloplasmin exhibits oxidase activity, which is associated with possible oxidation of Fe(II) into Fe(III), therefore assisting in its transport in the
1212:
4788:
4651:
4596:
4541:
4461:
1600:(right), two extremely different molecules when it comes to function, are quite similar when it comes to its atomic shape. There are only three major structural differences; a
1632:
ring. However, the magnesium ion is not directly involved in the photosynthetic function and can be replaced by other divalent ions with little loss of activity. Rather, the
1859:
residues involved in the binding are in positions 1, 3, 5, 7 and 9 of the polypeptide chain. At position 12, there is a glutamate or aspartate ligand that behaves as a
4212:
Aoki K, Murayama K, Hu NH (2017). "Chapter 7. Solid State
Structures of Lead Complexes with Relevance for Biological Systems". In Astrid S, Helmut S, Sigel RK (eds.).
1092:
attack by the negatively-charged hydroxide portion on carbon dioxide proceeds rapidly. The catalytic cycle produces the bicarbonate ion and the hydrogen ion as the
3578:
Parkin, Alison (2014). "Understanding and
Harnessing Hydrogenases, Biological Dihydrogen Catalysts". In Kroneck, Peter M. H.; Sosa Torres, Martha E. (eds.).
2251:
3272:
4953:
4949:
5090:
4882:
2663:
Cangelosi V, Ruckthong L, Pecoraro VL (2017). "Chapter 10. Lead(II) Binding in
Natural and Artificial Proteins". In Astrid S, Helmut S, Sigel RK (eds.).
507:
is another iron-containing oxygen carrier. The oxygen binding site is a binuclear iron center. The iron atoms are coordinated to the protein through the
353:, virtually all amino acid residues have been shown to bind metal centers. The peptide backbone also provides donor groups; these include deprotonated
63:. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding
5287:
2988:, Guss JM, Murata M, Norris VA, Ramshaw JA, Venkatappa MP (1978). "X-Ray Crystal-Structure Analysis of Plastocyanin at 2.7 Å Resolution".
1973:: one contains iron and molybdenum, the other contains iron and nickel. Parallels and differences in catalytic strategies have been reviewed.
4819:
4764:
4723:
4682:
4627:
4572:
4517:
4484:
4437:
4378:
4319:
4270:
4188:
3595:
3523:
3498:
3341:
3050:
2968:
2943:
2903:
2733:
2539:
2374:
2338:
768:
463:
or in muscle. In hemoglobin the four subunits show a cooperativity effect that allows for easy oxygen transfer from hemoglobin to myoglobin.
4802:
ten Brink, Felix (2014). "Living on
Acetylene. A Primordial Energy Source". In Kroneck, Peter M. H.; Sosa Torres, Martha E. (eds.).
1564:
1543:. The activity of Ni-SOD involves nickel(III), an unusual oxidation state for this element. The active site nickel geometry cycles from
325:
residues of the protein. These donor groups are often provided by side-chains on the amino acid residues. Especially important are the
851:
4945:
4941:
4229:
3438:
2680:
787:) from an axial methionine forms the apex. The distortion occurs in the bond lengths between the copper and sulfur ligands. The Cu−S
1544:
448:
5292:
3231:
Research in
Experimental Medicine. Zeitschrift für die Gesamte Experimentelle Medizin Einschliesslich Experimenteller Chirurgie
1084:
units. The fourth coordination site is occupied by a water molecule. The coordination sphere of the zinc ion is approximately
1072:. The structure of the active site in carbonic anhydrases is well known from a number of crystal structures. It consists of a
106:
are bound to proteins. For instance, the relatively high concentration of iron in the human body is mostly due to the iron in
5009:
4875:
2291:
1783:
1516:
1085:
1252:
that are involved in transporting the electrons needed to reduce the nitrogen, and an abundant energy source in the form of
4665:
Peacock AF, Pecoraro V (2013). "Natural and
Artificial Proteins Containing Cadmium". In Sigel A, Sigel H, Sigel RK (eds.).
4500:
Sydor AM, Zambie DB (2013). "Chapter 11. Nickel
Metallomics: General Themes Guiding Nickel Homeostasis". In Banci L (ed.).
2522:
Carver PL (2013). "Metal Ions and
Infectious Diseases. An Overview from the Clinic". In Sigel A, Sigel H, Sigel RK (eds.).
3186:
Rodríguez E, Díaz C (December 1995). "Iron, copper and zinc levels in urine: relationship to various individual factors".
1970:
390:
These are the second stage product of protein hydrolysis obtained by treatment with slightly stronger acids and alkalies.
103:
2813:
Karlin K, Cruse RW, Gultneh Y, Farooq A, Hayes JC, Zubieta J (1987). "Dioxygen–copper reactivity. Reversible binding of O
2321:
Banci L (2013). "Metallomics and the Cell: Some
Definitions and General Comments". In Sigel A, Sigel H, Sigel RK (eds.).
1667:, and is very reactive and allows an electron to be transferred to acceptors that are adjacent to the chlorophyll in the
4931:
2115:
3454:
Chan MK, Kim J, Rees DC (May 1993). "The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures".
2479:
Waldron KJ, Robinson NJ (January 2009). "How do bacterial cells ensure that metalloproteins get the correct metal?".
652:
group. The differences between those cytochromes lies in the different side-chains. For instance cytochrome a has a
493:
the iron atom lies above the plane of the ring. This change in spin state is a cooperative effect due to the higher
1956:, a structural module in which a region of protein folds around a zinc ion. The zinc does not directly contact the
833:
4868:
4555:
Vest KE, Hashemi HF, Cobine PA (2013). "Chapter 13. The Copper Metallome in Eukaryotic Cells". In Banci L (ed.).
3276:
1902:
549:. They are second only to hemoglobin in biological popularity of use in oxygen transport. On oxygenation the two
5282:
5162:
4849:
2091:
2087:
1763:
1184:
1766:
is the most studied ribozyme which has three metals participating in catalysis. Other known ribozymes include
694:
4420:
Cracan V, Banerjee R (2013). "Chapter 10 Cobalt and Corrinoid Transport and Biochemistry". In Banci L (ed.).
1871:
of the calcium ion contains only carboxylate oxygen atoms and no nitrogen atoms. This is consistent with the
5175:
5067:
4894:
2136:
2047:
1981:
1717:
553:(I) atoms at the active site are oxidized to copper(II) and the dioxygen molecules are reduced to peroxide,
474:
it is sometimes incorrectly stated that the oxygenated species contains iron(III). It is now known that the
365:
60:
1164:
5075:
4917:
2246:
1276:
1256:
950:
Metalloenzymes all have one feature in common, namely that the metal ion is bound to the protein with one
3357:
527:
by hemerythrin is accompanied by two-electron oxidation of the reduced binuclear center to produce bound
5085:
5080:
4927:
3229:
Schümann K, Schäfer SG, Forth W (1986). "Iron absorption and biliary excretion of transferrin in rats".
2725:
2152:
2095:
2006:
1309:. The precise structure of the active site has been difficult to determine. It appears to contain a MoFe
1287:
981:
954:
874:. The exact nature of the binding site has not yet been determined. The iron appears to be present as a
3950:"A catalytic beacon sensor for uranium with parts-per-trillion sensitivity and millionfold selectivity"
3429:. Advances in chemistry, Symposium series no. 535. Washington, DC: American Chemical Society. pp.
965:
is crucial. The metal ion is usually located in a pocket whose shape fits the substrate. The metal ion
4993:
4253:
Romani, Andrea M. P. (2013). "Magnesium Homeostasis in Mammalian Cells". In Banci, Lucia (ed.).
4020:
3961:
3867:
3675:
3628:
3540:
3387:
3195:
2999:
2576:
1949:
1652:
1458:
1390:
1093:
494:
4706:
Freisinger EF, Vasac M (2013). "Cadmium in Metallothioneins". In Sigel A, Sigel H, Sigel RK (eds.).
2402:
Andreini C, Banci L, Bertini I, Rosato A (November 2006). "Zinc through the three domains of life".
5167:
4973:
4855:
3421:
Orme-Johnson, W. H. (1993). Steifel, E. I.; Coucouvannis, D.; Newton, D. C. (eds.).
2217:
1905:. In general, when calcium rises, the muscles contract and, when calcium falls, the muscles relax.
1868:
1851:
loop protein domain, the calcium ion is coordinated in a pentagonal bipyramidal configuration. Six
1775:
1337:
1260:
1249:
906:. Iron is actually excreted in urine and is also concentrated in bile which is excreted in feces.
804:
92:
5189:
4782:
4645:
4590:
4535:
4455:
3403:
3254:
3060:
3015:
2504:
2256:
2128:
2018:
1415:
1069:
986:
674:
enzymes perform the function of inserting an oxygen atom into a C−H bond, an oxidation reaction.
1389:. Otherwise, the superoxide ion must be destroyed before it does unwanted damage in a cell. The
3430:
2778:
Wirstam M, Lippard SJ, Friesner RA (April 2003). "Reversible dioxygen binding to hemerythrin".
1039:
This reaction is very slow in the absence of a catalyst, but quite fast in the presence of the
5260:
5019:
5001:
4825:
4815:
4770:
4760:
4729:
4719:
4688:
4678:
4633:
4623:
4578:
4568:
4523:
4513:
4480:
4443:
4433:
4402:
4384:
4374:
4343:
4325:
4315:
4302:
Roth J, Ponzoni S, Aschner M (2013). "Manganese Homeostasis and Transport". In Banci L (ed.).
4284:
4276:
4266:
4235:
4225:
4194:
4184:
4153:
4118:
4083:
4048:
4009:"In vitro selection of a sodium-specific DNAzyme and its application in intracellular sensing"
3989:
3930:
3895:
3836:
3787:
3752:
3703:
3644:
3601:
3591:
3560:
3519:
3494:
3471:
3434:
3337:
3314:
3246:
3211:
3168:
3150:
3119:
3046:
2964:
2939:
2899:
2868:
2819:
2795:
2729:
2696:
2676:
2645:
2604:
2545:
2535:
2496:
2461:
2419:
2370:
2344:
2334:
2276:
2193:
2140:
2083:
1636:
is absorbed by the chlorin ring, whose electronic structure is well-adapted for this purpose.
1419:
1236:
1224:
1168:
1052:
970:
899:
760:
744:
629:
609:
4361:
Dlouhy AC, Outten CE (2013). "The Iron Metallome in Eukaryotic Organisms". In Banci L (ed.).
1987:
Some other metalloenzymes are given in the following table, according to the metal involved.
1917:, is the protein complex to which calcium binds to trigger the production of muscular force.
726:
of the iron atom changes between the +2 and +3 states. In both oxidation states the metal is
4807:
4752:
4711:
4670:
4615:
4560:
4505:
4425:
4392:
4366:
4333:
4307:
4258:
4217:
4176:
4145:
4110:
4075:
4038:
4028:
3979:
3969:
3922:
3885:
3875:
3826:
3818:
3779:
3742:
3734:
3693:
3683:
3636:
3583:
3552:
3463:
3422:
3395:
3306:
3238:
3203:
3158:
3109:
3099:
3038:
3007:
2990:
2876:
2827:
2787:
2760:
2717:
2686:
2668:
2635:
2594:
2584:
2527:
2488:
2453:
2411:
2326:
2296:
2201:
2156:
1895:
1779:
1462:
1006:
942:
Osteopontin is involved in mineralization in the extracellular matrices of bones and teeth.
641:
624:(II), on the other hand, can easily be oxidized to iron(III). This functionality is used in
456:
3086:
Anderson BF, Baker HM, Dodson EJ, Norris GE, Rumball SV, Waters JM, Baker EN (April 1987).
1167:, a process that is energetically expensive in organic reactions. The metal ion lowers the
5023:
4845:
3072:
2227:
2197:
2176:
1767:
1397:
1374:
1180:
756:
723:
671:
661:
613:
490:
2438:
1836:
is an example of a signal-transduction protein. It is a small protein that contains four
4149:
4024:
3965:
3871:
3679:
3632:
3391:
3199:
3003:
2580:
1790:) and the large subunit of ribosomes. Several classes of ribozymes have been described.
5039:
4747:
Mendel, Ralf R. (2013). "Chapter 15. Metabolism of Molybdenum". In Banci, Lucia (ed.).
4397:
4338:
4043:
4008:
3984:
3949:
3831:
3806:
3747:
3722:
3378:
Hodgkin, D. C. (1965). "The Structure of the Corrin Nucleus from X-ray Analysis".
3163:
3138:
2691:
2599:
2564:
2205:
2160:
2014:
1891:
1879:
1771:
1621:
1204:
1010:
637:
617:
572:
546:
361:
oxygen centers. Lead(II) binding in natural and artificial proteins has been reviewed.
84:
64:
4114:
3310:
3207:
3114:
3087:
2457:
1527:
ions for stabilization and is activated by copper chaperone for superoxide dismutase (
5276:
5152:
5105:
5057:
3926:
3890:
3855:
3783:
3698:
3663:
3423:
2281:
1856:
1852:
1793:
1758:
1660:
1656:
1648:
1644:
1386:
1125:
1014:
915:
895:
894:. The human body has no controlled mechanism for excretion of iron. This can lead to
887:
665:
633:
568:
498:
483:
3407:
3035:
Spectroscopic Studies of Active Sites. Blue Copper and Electronic Structural Analogs
1925:
1898:, muscular force production is controlled primarily by changes in the intracellular
1736:
5157:
5147:
5115:
3258:
3019:
2985:
2508:
2271:
2164:
1797:
1664:
1370:
1089:
925:
749:
739:
576:
487:
364:
In addition to donor groups that are provided by amino acid residues, many organic
4756:
4619:
4564:
4509:
4429:
3723:"New classes of self-cleaving ribozymes revealed by comparative genomics analysis"
3721:
Weinberg Z, Kim PB, Chen TH, Li S, Harris KA, Lünse CE, Breaker RR (August 2015).
531:(OOH). The mechanism of oxygen uptake and release have been worked out in detail.
401:, which is the principal oxygen-carrier in humans, has four subunits in which the
4715:
4674:
3822:
1863:
ligand, providing two oxygen atoms. The ninth residue in the loop is necessarily
928:
in association with transferrin, which can carry iron only in the Fe(III) state.
5142:
5095:
4811:
4370:
4311:
4262:
4180:
4007:
Torabi SF, Wu P, McGhee CE, Chen L, Hwang K, Zheng N, Cheng J, Lu Y (May 2015).
3587:
2531:
2389:
2330:
2286:
2266:
2231:
2111:
2063:
1953:
1929:
1914:
1787:
1754:
1680:
1668:
1613:
1597:
1584:
1580:
1454:
1232:
1228:
1149:
1088:. The positively-charged zinc ion polarizes the coordinated water molecule, and
962:
937:
903:
879:
843:
719:
508:
504:
475:
440:
436:
406:
372:
342:
4013:
Proceedings of the National Academy of Sciences of the United States of America
3954:
Proceedings of the National Academy of Sciences of the United States of America
3948:
Liu J, Brown AK, Meng X, Cropek DM, Istok JD, Watson DB, Lu Y (February 2007).
3860:
Proceedings of the National Academy of Sciences of the United States of America
3668:
Proceedings of the National Academy of Sciences of the United States of America
3092:
Proceedings of the National Academy of Sciences of the United States of America
3042:
771:. The trigonal plane of the pyramidal base is composed of two nitrogen atoms (N
714:. The active site contains an iron ion coordinated by the sulfur atoms of four
32:
5222:
5110:
5100:
4963:
4221:
2752:
2672:
2188:
2010:
1977:
1833:
1593:
1528:
1382:
1346:
1245:
1196:
875:
699:
686:
645:
625:
596:
584:
534:
467:
398:
322:
107:
100:
37:
4774:
4637:
4582:
4527:
4447:
4388:
4329:
4280:
4101:
Chin D, Means AR (August 2000). "Calmodulin: a prototypical calcium sensor".
3688:
3154:
2565:"Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals"
17:
5217:
5212:
5047:
5033:
4033:
3974:
3640:
3467:
2624:"Metalloproteomics, metalloproteomes, and the annotation of metalloproteins"
2301:
2071:
2038:
2001:
1937:
1860:
1697:
1625:
1601:
1589:
1520:
1306:
1253:
1200:
1192:
1081:
1077:
1040:
994:
990:
966:
891:
829:
808:
792:
727:
601:
542:
520:
516:
512:
471:
444:
432:
420:
416:
412:
346:
330:
326:
142:
4829:
4733:
4692:
4610:
Maret W (2013). "Chapter 14 Zinc and the Zinc Proteome". In Banci L (ed.).
4406:
4347:
4288:
4239:
4216:. Metal Ions in Life Sciences. Vol. 17. de Gruyter. pp. 123–200.
4198:
4122:
4052:
3993:
3880:
3840:
3756:
3707:
3605:
3564:
3399:
3172:
3104:
2799:
2700:
2667:. Metal Ions in Life Sciences. Vol. 17. de Gruyter. pp. 271–318.
2649:
2608:
2549:
2500:
2423:
2348:
1457:
reaction. It involves both oxidation and reduction of superoxide ions. The
443:
pocket. This is important as without it the iron(II) would be irreversibly
4157:
4087:
3934:
3899:
3791:
3738:
3648:
3475:
3318:
3250:
3215:
3123:
2465:
1882:
system by acting as a diffusible second messenger to the initial stimuli.
1187:. It consists of a cobalt(II) ion coordinated to four nitrogen atoms of a
4710:. Metal Ions in Life Sciences. Vol. 11. Springer. pp. 339–372.
4669:. Metal Ions in Life Sciences. Vol. 11. Springer. pp. 303–337.
4306:. Metal Ions in Life Sciences. Vol. 12. Springer. pp. 169–201.
4136:
Berg JM (1990). "Zinc finger domains: hypotheses and current knowledge".
3664:"Three metal ions at the active site of the Tetrahymena group I ribozyme"
2261:
2212:
2180:
2059:
2043:
2031:
2026:
1941:
1906:
1750:
1687:
1640:
1609:
1378:
1366:
1241:
1176:
951:
883:
871:
715:
707:
528:
479:
428:
358:
350:
338:
334:
310:
4804:
The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment
4365:. Metal Ions in Life Sciences. Vol. 12. Springer. pp. 241–78.
4257:. Metal Ions in Life Sciences. Vol. 12. Springer. pp. 69–118.
4173:
The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment
3619:
Pyle AM (August 1993). "Ribozymes: a distinct class of metalloenzymes".
3582:. Metal Ions in Life Sciences. Vol. 14. Springer. pp. 99–124.
3580:
The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment
2880:
2831:
2764:
2589:
2492:
1227:
is an energy-intensive process, as it involves breaking the very stable
486:
the iron atom is located in the plane of the porphyrin ring, but in the
5253:
5197:
4909:
4806:. Metal Ions in Life Sciences. Vol. 14. Springer. pp. 15–35.
4175:. Metal Ions in Life Sciences. Vol. 14. Springer. pp. 37–69.
3913:
Breaker RR, Joyce GF (December 1994). "A DNA enzyme that cleaves RNA".
3770:
Breaker RR, Joyce GF (December 1994). "A DNA enzyme that cleaves RNA".
3242:
2171:
2132:
1899:
1864:
1848:
1841:
1837:
1629:
1532:
1280:
711:
682:
580:
538:
76:
56:
3556:
2791:
2526:. Metal Ions in Life Sciences. Vol. 13. Springer. pp. 1–28.
2415:
2325:. Metal Ions in Life Sciences. Vol. 12. Springer. pp. 1–13.
382:
protein. Inorganic ligands such as sulfide and oxide are also common.
5227:
5202:
5136:
5132:
5128:
5124:
4983:
4891:
3662:
Shan S, Yoshida A, Sun S, Piccirilli JA, Herschlag D (October 1999).
3011:
2640:
2623:
2123:
2107:
2102:
2078:
2067:
1809:
1805:
1801:
1740:
The active site structures of the three types of hydrogenase enzymes.
1633:
1540:
1512:
1362:
1264:
1188:
1156:
1145:
958:
921:
847:
764:
703:
657:
653:
550:
409:
375:
318:
314:
250:
223:
196:
88:
4079:
3543:(June 2004). "Nickel superoxide dismutase structure and mechanism".
3297:
Lindskog S (1997). "Structure and mechanism of carbonic anhydrase".
2365:
Shriver DF, Atkins PW (1999). "Charper 19, Bioinorganic chemistry".
4860:
1825:
1924:
1910:
1735:
1694:
1336:
980:
681:
605:
424:
354:
80:
31:
5232:
5207:
5120:
2147:
2054:
1933:
1872:
1605:
1536:
1524:
1318:
1073:
998:
867:
649:
621:
460:
402:
379:
277:
169:
45:
41:
4864:
1163:) groups between two molecules, which involves the breaking of
478:
nature of these species is because the iron(II) atom is in the
368:
function as ligands. Perhaps most famous are the tetradentate N
2524:
Interrelations between Essential Metal Ions and Human Diseases
1957:
1608:(Fe) in hemoglobin. Additionally, chlorophyll has an extended
660:
prosthetic group. These differences result in different Fe/Fe
2740:
Fig.25.7, p 1100 illustrates the structure of deoxyhemoglobin
1361:
is generated in biological systems by reduction of molecular
455:
is such that oxygen is taken up or released depending on the
67:
although there may be up to 3000 human zinc metalloproteins.
1867:
due to the conformational requirements of the backbone. The
1211:-methylation reactions, such as the reaction carried out by
1411:
1129:
722:. Rubredoxins perform one-electron transfer processes. The
439:, has only one such unit. The active site is located in a
309:
In metalloproteins, metal ions are usually coordinated by
4856:
Catherine Drennan's Seminar: Snapshots of Metalloproteins
4066:
Stevens FC (August 1983). "Calmodulin: an introduction".
2750:
Stenkamp, R. E. (1994). "Dioxygen and hemerythrin".
1976:
Pb (lead) can replace Ca (calcium) as, for example, with
2894:
Messerschmidt A, Huber R, Wieghardt K, Poulos T (2001).
1068:
A reaction similar to this is almost instantaneous with
4751:. Metal Ions in Life Sciences. Vol. 12. Springer.
4614:. Metal Ions in Life Sciences. Vol. 12. Springer.
4559:. Metal Ions in Life Sciences. Vol. 12. Springer.
4504:. Metal Ions in Life Sciences. Vol. 12. Springer.
4424:. Metal Ions in Life Sciences. Vol. 12. Springer.
803:
bonding destabilizes the Cu(II) form and increases the
114:
Metal concentrations in humans organs (ppm = μg/g ash)
2961:
Cytochrome P450 Structure, Mechanism, and Biochemistry
648:. The iron atom in most cytochromes is contained in a
640:
that cannot easily be performed by the limited set of
4138:
Annual Review of Biophysics and Biophysical Chemistry
3088:"Structure of human lactoferrin at 3.2-A resolution"
2921:
Cytochrome c: Structural and Physicochemical Aspects
1341:
Structure of a human superoxide dismutase 2 tetramer
1155:(also known as cobalamin) catalyzes the transfer of
5245:
5188:
5066:
4908:
4901:
4479:. Metal Ions in Life Sciences. Vol. 2. Wiley.
3336:. Metal Ions in Life Sciences. Vol. 6. Wiley.
3139:"The Regulation of Iron Absorption and Homeostasis"
2938:. Metal Ions in Life Sciences. Vol. 3. Wiley.
2817:and CO to a phenoxo-bridged dicopper(I) complex".
1693:uptake, but while the and hydrogenases are true
1377:. These properties render the superoxide ion very
664:such that various cytochromes are involved in the
575:) is an oxygen-binding hemeprotein present in the
4787:: CS1 maint: DOI inactive as of September 2024 (
4650:: CS1 maint: DOI inactive as of September 2024 (
4595:: CS1 maint: DOI inactive as of September 2024 (
4540:: CS1 maint: DOI inactive as of September 2024 (
4460:: CS1 maint: DOI inactive as of September 2024 (
4068:Canadian Journal of Biochemistry and Cell Biology
3807:"Pursuing DNA catalysts for protein modification"
3491:Superoxide Dismutase: 349 (Methods in Enzymology)
3188:Journal of Trace Elements in Medicine and Biology
3539:Barondeau DP, Kassmann CJ, Bruns CK, Tainer JA,
1639:Initially, the absorption of a photon causes an
1393:enzymes perform this function very efficiently.
1235:catalyze the process. One such enzyme occurs in
878:product such as FeO(OH). Iron is transported by
423:residue. The sixth coordination site contains a
3425:Molybdenum enzymes, cofactors and model systems
2936:The Ubiquitous Roles of Cytochrome 450 Proteins
1659:in which there are two electrons with parallel
1263:between the bacteria and a host plant, often a
75:It is estimated that approximately half of all
1267:. The reaction may be written symbolically as
1244:. There are three components to its action: a
730:, which helps to minimize structural changes.
632:vectors. The presence of the metal ion allows
4876:
2252:Evolution of metal ions in biological systems
1774:, and several small viral ribozymes (such as
1453:In biology this type of reaction is called a
87:, such as storage and transport of proteins,
8:
3518:(in German). Berlin: Springer. p. 123.
1195:group. In the resting state there is a Co−C
1171:for the process by forming a transient Co−CH
4214:Lead: Its Effects on Environment and Health
3856:"A general purpose RNA-cleaving DNA enzyme"
3514:Heinrich P, Löffler G, Petrides PE (2006).
3334:Metal–carbon bonds in enzymes and cofactors
2665:Lead: Its Effects on Environment and Health
969:reactions that are difficult to achieve in
4905:
4883:
4869:
4861:
4477:Nickel and Its Surprising Impact in Nature
1716:the hydrogenases catalyze the reversible
779:) from separate histidines and a sulfur (S
755:Plastocyanin is one of the family of blue
27:Protein that contains a metal ion cofactor
4848:at the U.S. National Library of Medicine
4475:Sigel A, Sigel H, Sigel RK, eds. (2008).
4396:
4337:
4042:
4032:
3983:
3973:
3889:
3879:
3830:
3746:
3697:
3687:
3332:Sigel A, Sigel H, Sigel RK, eds. (2008).
3162:
3113:
3103:
3033:Solomon EI, Gewirth AA, Cohen SL (1986).
2934:Sigel A, Sigel H, Sigel RK, eds. (2007).
2690:
2639:
2598:
2588:
2369:(3rd ed.). Oxford University Press.
1207:compound, which explains its function in
1183:and co-workers, for which she received a
807:of the protein. The blue color (597
2858:-peroxo dinuclear copper(II) complexes,
2780:Journal of the American Chemical Society
2563:Wang, MS; Hoegler, KH; Hecht, M (2019).
1996:Examples of enzymes containing this ion
1989:
1840:motifs, each of which is able to bind a
1824:
1604:atom (Mg) in chlorophyll, as opposed to
1588:
767:-binding site is described as distorted
743:
656:prosthetic group and cytochrome b has a
112:
2313:
1191:ring and a fifth nitrogen atom from an
4780:
4708:Cadmium: From Toxicity to Essentiality
4667:Cadmium: From Toxicity to Essentiality
4643:
4588:
4533:
4453:
3068:
3058:
2712:
2710:
405:(II) ion is coordinated by the planar
3273:"Biliary excretion of waste products"
850:and the copper site geometry becomes
828:In the reduced form of plastocyanin,
386:Storage and transport metalloproteins
7:
2360:
2358:
1620:Chlorophyll plays a crucial role in
1523:residues. This enzyme also contains
1461:(SOD) group of enzymes increase the
612:as few organic molecules can act as
349:. Given the diversity of the metallo
4150:10.1146/annurev.bb.19.060190.002201
3854:Santoro SW, Joyce GF (April 1997).
3358:"The Nobel Prize in Chemistry 1964"
3037:. Vol. 307. pp. 236–266.
2446:Current Opinion in Chemical Biology
1816:Signal-transduction metalloproteins
1329:clusters joined by sulfur bridges.
882:whose binding site consists of two
811:peak absorption) is due to the Cu−S
718:residues forming an almost regular
501:of Fe in the oxyhemoglobin moiety.
1936:ion (green) is coordinated by two
1808:-specific) and the NaA43 DNAzyme (
1515:, as Cu(II) or Cu(I), coordinated
1511:In human SOD, the active metal is
898:problems in patients treated with
832:-87 will become protonated with a
537:carry oxygen in the blood of most
431:molecule. By contrast the protein
25:
1381:and are deployed to advantage by
799:(282 pm). The elongated Cu−S
305:Coordination chemistry principles
2392:in Uniprot, accessed 12 Jan 2018
1800:-specific), the CA1-3 DNAzymes (
1663:. This species is, in effect, a
1231:between the nitrogen atoms. The
1225:fixation of atmospheric nitrogen
1203:. This is a naturally occurring
702:is an electron-carrier found in
3299:Pharmacology & Therapeutics
3143:The Clinical Biochemist Reviews
2919:Moore GR, Pettigrew GW (1990).
1952:contain a structure known as a
1575:Chlorophyll-containing proteins
1567:Ni(III) with an added axial His
1219:Nitrogenase (nitrogen fixation)
44:cofactor, containing the metal
3137:Wallace, Daniel F (May 2016).
2959:Ortiz de Montellano P (2005).
2292:Plant matrix metalloproteinase
858:Metal-ion storage and transfer
583:, particularly certain marine
1:
5288:Medicinal inorganic chemistry
4757:10.1007/978-94-007-5561-10_15
4620:10.1007/978-94-007-5561-10_14
4565:10.1007/978-94-007-5561-10_12
4510:10.1007/978-94-007-5561-10_11
4430:10.1007/978-94-007-5561-10_10
4115:10.1016/S0962-8924(00)01800-6
3811:Accounts of Chemical Research
3311:10.1016/S0163-7258(96)00198-2
3208:10.1016/S0946-672X(11)80025-8
2458:10.1016/S1367-5931(98)80056-2
1971:carbon monoxide dehydrogenase
1804:-specific), the 39E DNAzyme (
1259:. This last is provided by a
993:residues are shown in green,
791:contact is shorter (207
636:to perform functions such as
4716:10.1007/978-94-007-5179-8_11
4675:10.1007/978-94-007-5179-8_10
3927:10.1016/1074-5521(94)90014-0
3823:10.1021/acs.accounts.5b00090
3784:10.1016/1074-5521(94)90014-0
3516:Biochemie und Pathobiochemie
2481:Nature Reviews. Microbiology
2437:Thomson AJ, Gray HB (1998).
2404:Journal of Proteome Research
1655:from the singlet state to a
1555:) and backbone nitrogen (His
783:) from a cysteine. Sulfur (S
608:reactions are not common in
4812:10.1007/978-94-017-9269-1_2
4371:10.1007/978-94-007-5561-1_8
4312:10.1007/978-94-007-5561-1_6
4263:10.1007/978-94-007-5561-1_4
4181:10.1007/978-94-017-9269-1_3
3588:10.1007/978-94-017-9269-1_5
2896:Handbook of Metalloproteins
2866:) (R = isopropyl and Ph)".
2532:10.1007/978-94-007-7500-8_1
2331:10.1007/978-94-007-5561-1_1
2116:Methyl-coenzyme M reductase
1875:nature of the calcium ion.
1199:with the 5′ carbon atom of
1179:was famously determined by
1175:bond. The structure of the
920:Ceruloplasmin is the major
902:, as, for instance, with β-
5309:
3043:10.1021/bk-1986-0307.ch016
2963:(3rd ed.). Springer.
1745:Ribozyme and deoxyribozyme
1704:oxidation and H reduction
1678:
1614:aliphatic cyclic structure
1578:
1547:Ni(II), with thiolate (Cys
1410:. In solutions at neutral
1124:favouring dissociation of
1080:nitrogen atoms from three
997:in red and white, and the
935:
913:
870:is stored as iron(III) in
825:) charge transfer occurs.
737:
692:
668:electron transport chain.
594:
59:that contains a metal ion
4222:10.1515/9783110434330-007
3805:Silverman SK (May 2015).
2722:Chemistry of the Elements
2720:; Earnshaw, Alan (1997).
2673:10.1515/9783110434330-010
2622:Maret W (February 2010).
1248:atom at the active site,
1076:ion coordinated by three
989:. The three coordinating
523:residues. The uptake of O
4850:Medical Subject Headings
4749:Metallomics and the Cell
4612:Metallomics and the Cell
4557:Metallomics and the Cell
4502:Metallomics and the Cell
4422:Metallomics and the Cell
4363:Metallomics and the Cell
4304:Metallomics and the Cell
4255:Metallomics and the Cell
3689:10.1073/pnas.96.22.12299
3489:Packer, L., ed. (2002).
2439:"Bioinorganic chemistry"
2390:Human reference proteome
2323:Metallomics and the Cell
2092:Methylmalonyl-CoA mutase
2088:Methionyl aminopeptidase
1982:metallocarboxypeptidases
1418:to molecular oxygen and
1400:of the oxygen atoms is −
1185:Nobel Prize in Chemistry
846:prevents it acting as a
815:bond where S(pπ) to Cu(d
451:for the formation of HbO
55:is a generic term for a
4759:(inactive 2024-09-12).
4622:(inactive 2024-09-12).
4567:(inactive 2024-09-12).
4512:(inactive 2024-09-12).
4432:(inactive 2024-09-12).
4034:10.1073/pnas.1420361112
3975:10.1073/pnas.0607875104
3915:Chemistry & Biology
3772:Chemistry & Biology
3727:Nature Chemical Biology
3641:10.1126/science.7688142
3468:10.1126/science.8484118
2137:Nitrous-oxide reductase
2048:Oxygen-evolving complex
1969:There are two types of
1880:intracellular signaling
571:(as the larger carrier
495:crystal field splitting
5293:Bioinorganic chemistry
4103:Trends in Cell Biology
3881:10.1073/pnas.94.9.4262
3400:10.1098/rspa.1965.0219
3105:10.1073/pnas.84.7.1769
2247:Bioinorganic chemistry
1945:
1830:
1741:
1617:
1342:
1002:
752:
690:
378:incorporated into the
49:
3739:10.1038/nchembio.1846
2726:Butterworth-Heinemann
2718:Greenwood, Norman N.
2153:Alcohol dehydrogenase
2096:Isobutyryl-CoA mutase
2007:Glucose 6-phosphatase
1980:or Zn (zinc) as with
1950:transcription factors
1928:
1921:Transcription factors
1828:
1739:
1643:to be excited into a
1592:
1414:, the superoxide ion
1369:, so it behaves as a
1365:. It has an unpaired
1340:
1305:stands for inorganic
1261:mutualistic symbiosis
984:
759:that are involved in
747:
685:
321:centers belonging to
35:
1965:Other metalloenzymes
1653:intersystem crossing
1616:off the macrocycle.
1459:superoxide dismutase
1391:superoxide dismutase
1333:Superoxide dismutase
1279:+ 8 e → 2
1250:iron–sulfur clusters
628:, which function as
449:equilibrium constant
4025:2015PNAS..112.5903T
3966:2007PNAS..104.2056L
3872:1997PNAS...94.4262S
3680:1999PNAS...9612299S
3633:1993Sci...261..709P
3392:1965RSPSA.288..294H
3200:1995JTEMB...9..200R
3004:1978Natur.272..319C
2923:. Berlin: Springer.
2881:10.1021/ja00030a025
2832:10.1021/ja00243a019
2765:10.1021/cr00027a008
2590:10.3390/life9010008
2581:2019Life....9....8W
2493:10.1038/nrmicro2057
2367:Inorganic chemistry
2218:Acetylene hydratase
1869:coordination sphere
1749:Since discovery of
1647:of the Q band. The
1571:side chain ligand.
1373:. It is a powerful
1213:methionine synthase
961:, the shape of the
748:The copper site in
695:Iron–sulfur protein
419:nitrogen atom of a
345:groups provided by
115:
99:Most metals in the
93:signal transduction
3493:. Academic Press.
3243:10.1007/BF01852047
2129:Cytochrome oxidase
2019:Poly(A) polymerase
1946:
1831:
1742:
1618:
1612:and an additional
1499:+ 2 H → M + H
1343:
1140:-dependent enzymes
1070:carbonic anhydrase
1003:
987:carbonic anhydrase
977:Carbonic anhydrase
957:site. As with all
900:blood transfusions
769:trigonal pyramidal
753:
691:
447:to iron(III). The
113:
50:
5270:
5269:
5241:
5240:
4821:978-94-017-9268-4
4766:978-94-007-5561-1
4725:978-94-007-5178-1
4684:978-94-007-5178-1
4629:978-94-007-5561-1
4574:978-94-007-5561-1
4519:978-94-007-5561-1
4486:978-0-470-01671-8
4439:978-94-007-5561-1
4380:978-94-007-5561-1
4321:978-94-007-5561-1
4272:978-94-007-5561-1
4190:978-94-017-9268-4
3674:(22): 12299–304.
3597:978-94-017-9268-4
3557:10.1021/bi0496081
3525:978-3-540-32680-9
3500:978-0-12-182252-1
3386:(1414): 294–305.
3343:978-1-84755-915-9
3052:978-0-8412-0971-8
2998:(5651): 319–324.
2970:978-0-306-48324-0
2945:978-0-470-01672-5
2905:978-0-471-62743-2
2869:J. Am. Chem. Soc.
2820:J. Am. Chem. Soc.
2792:10.1021/ja017692r
2735:978-0-08-037941-8
2541:978-94-007-7499-5
2416:10.1021/pr0603699
2376:978-0-19-850330-9
2340:978-94-007-5561-1
2277:Metalloproteinase
2237:
2236:
2194:Nitrate reductase
2141:Nitrite reductase
2084:Nitrile hydratase
1940:residues and two
1420:hydrogen peroxide
1416:disproportionates
1385:to kill invading
1169:activation energy
971:organic chemistry
761:electron transfer
642:functional groups
630:electron-transfer
610:organic chemistry
511:side chains of a
459:of oxygen in the
413:protoporphyrin IX
302:
301:
48:, shown in green.
36:The structure of
16:(Redirected from
5300:
4906:
4885:
4878:
4871:
4862:
4834:
4833:
4799:
4793:
4792:
4786:
4778:
4744:
4738:
4737:
4703:
4697:
4696:
4662:
4656:
4655:
4649:
4641:
4607:
4601:
4600:
4594:
4586:
4552:
4546:
4545:
4539:
4531:
4497:
4491:
4490:
4472:
4466:
4465:
4459:
4451:
4417:
4411:
4410:
4400:
4358:
4352:
4351:
4341:
4299:
4293:
4292:
4250:
4244:
4243:
4209:
4203:
4202:
4168:
4162:
4161:
4133:
4127:
4126:
4098:
4092:
4091:
4063:
4057:
4056:
4046:
4036:
4004:
3998:
3997:
3987:
3977:
3945:
3939:
3938:
3910:
3904:
3903:
3893:
3883:
3851:
3845:
3844:
3834:
3802:
3796:
3795:
3767:
3761:
3760:
3750:
3718:
3712:
3711:
3701:
3691:
3659:
3653:
3652:
3627:(5122): 709–14.
3616:
3610:
3609:
3575:
3569:
3568:
3536:
3530:
3529:
3511:
3505:
3504:
3486:
3480:
3479:
3451:
3445:
3444:
3428:
3418:
3412:
3411:
3375:
3369:
3368:
3366:
3365:
3360:. Nobelprize.org
3354:
3348:
3347:
3329:
3323:
3322:
3294:
3288:
3287:
3285:
3284:
3275:. Archived from
3269:
3263:
3262:
3226:
3220:
3219:
3183:
3177:
3176:
3166:
3134:
3128:
3127:
3117:
3107:
3083:
3077:
3076:
3070:
3066:
3064:
3056:
3030:
3024:
3023:
3012:10.1038/272319a0
2981:
2975:
2974:
2956:
2950:
2949:
2931:
2925:
2924:
2916:
2910:
2909:
2891:
2885:
2884:
2875:(4): 1277–1291.
2842:
2836:
2835:
2826:(9): 2668–2679.
2810:
2804:
2803:
2775:
2769:
2768:
2747:
2741:
2739:
2724:(2nd ed.).
2714:
2705:
2704:
2694:
2660:
2654:
2653:
2643:
2641:10.1039/b915804a
2619:
2613:
2612:
2602:
2592:
2560:
2554:
2553:
2519:
2513:
2512:
2476:
2470:
2469:
2443:
2434:
2428:
2427:
2399:
2393:
2387:
2381:
2380:
2362:
2353:
2352:
2318:
2297:Prosthetic group
2202:Xanthine oxidase
2157:Carboxypeptidase
1990:
1896:skeletal muscles
1712:⇌ 2 H + 2 e
1624:. It contains a
1565:square pyramidal
1498:
1497:
1496:
1480:
1479:
1478:
1463:rate of reaction
1437:
1436:
1435:
1409:
1408:
1404:
1360:
1359:
1358:
1119:
1118:
1117:
1063:
1062:
1061:
1007:aqueous solution
662:redox potentials
564:
563:
562:
457:partial pressure
337:substituents in
116:
21:
5308:
5307:
5303:
5302:
5301:
5299:
5298:
5297:
5283:Metalloproteins
5273:
5272:
5271:
5266:
5237:
5184:
5179:
5171:
5062:
5053:
5045:
5029:
5015:
5005:
4997:
4989:
4979:
4969:
4959:
4937:
4923:
4897:
4889:
4842:
4837:
4822:
4801:
4800:
4796:
4779:
4767:
4746:
4745:
4741:
4726:
4705:
4704:
4700:
4685:
4664:
4663:
4659:
4642:
4630:
4609:
4608:
4604:
4587:
4575:
4554:
4553:
4549:
4532:
4520:
4499:
4498:
4494:
4487:
4474:
4473:
4469:
4452:
4440:
4419:
4418:
4414:
4381:
4360:
4359:
4355:
4322:
4301:
4300:
4296:
4273:
4252:
4251:
4247:
4232:
4211:
4210:
4206:
4191:
4170:
4169:
4165:
4135:
4134:
4130:
4100:
4099:
4095:
4080:10.1139/o83-115
4065:
4064:
4060:
4006:
4005:
4001:
3947:
3946:
3942:
3912:
3911:
3907:
3853:
3852:
3848:
3804:
3803:
3799:
3769:
3768:
3764:
3720:
3719:
3715:
3661:
3660:
3656:
3618:
3617:
3613:
3598:
3577:
3576:
3572:
3551:(25): 8038–47.
3538:
3537:
3533:
3526:
3513:
3512:
3508:
3501:
3488:
3487:
3483:
3462:(5109): 792–4.
3453:
3452:
3448:
3441:
3420:
3419:
3415:
3380:Proc. R. Soc. A
3377:
3376:
3372:
3363:
3361:
3356:
3355:
3351:
3344:
3331:
3330:
3326:
3296:
3295:
3291:
3282:
3280:
3271:
3270:
3266:
3228:
3227:
3223:
3185:
3184:
3180:
3136:
3135:
3131:
3085:
3084:
3080:
3067:
3057:
3053:
3032:
3031:
3027:
2983:
2982:
2978:
2971:
2958:
2957:
2953:
2946:
2933:
2932:
2928:
2918:
2917:
2913:
2906:
2893:
2892:
2888:
2865:
2861:
2844:
2843:
2839:
2816:
2812:
2811:
2807:
2777:
2776:
2772:
2749:
2748:
2744:
2736:
2716:
2715:
2708:
2683:
2662:
2661:
2657:
2621:
2620:
2616:
2562:
2561:
2557:
2542:
2521:
2520:
2516:
2478:
2477:
2473:
2441:
2436:
2435:
2431:
2401:
2400:
2396:
2388:
2384:
2377:
2364:
2363:
2356:
2341:
2320:
2319:
2315:
2311:
2306:
2242:
2230:
2228:Metallothionein
2204:
2200:
2198:Sulfite oxidase
2196:
2179:
2177:Metallothionein
2163:
2159:
2155:
2139:
2135:
2131:
2114:
2110:
2094:
2090:
2086:
2070:
2066:
2062:
2046:
2013:
2009:
1967:
1923:
1888:
1823:
1818:
1768:group II intron
1747:
1731:
1723:
1711:
1703:
1691:
1683:
1677:
1610:isoprenoid tail
1587:
1579:Main articles:
1577:
1570:
1562:
1558:
1554:
1550:
1539:, manganese or
1506:
1502:
1495:
1492:
1491:
1490:
1488:
1487:Reduction: M +
1484:
1477:
1474:
1473:
1472:
1470:
1469:Oxidation: M +
1449:
1445:
1441:
1434:
1431:
1430:
1429:
1427:
1406:
1402:
1401:
1398:oxidation state
1375:oxidizing agent
1357:
1354:
1353:
1352:
1350:
1335:
1328:
1324:
1316:
1312:
1304:
1297:
1293:
1284:
1274:
1221:
1181:Dorothy Hodgkin
1174:
1162:
1153:
1142:
1139:
1116:
1113:
1112:
1111:
1109:
1107:
1103:
1060:
1057:
1056:
1055:
1053:
1050:
1035:
1031:
1027:
1023:
985:Active site of
979:
948:
940:
934:
918:
912:
865:
860:
852:trigonal planar
840:
824:
814:
805:redox potential
802:
798:
790:
786:
782:
778:
774:
763:reactions. The
757:copper proteins
742:
736:
724:oxidation state
697:
680:
672:Cytochrome P450
638:redox reactions
618:reducing agents
599:
593:
561:
558:
557:
556:
554:
526:
491:deoxyhemoglobin
454:
396:
394:Oxygen carriers
388:
371:
329:substituent in
307:
73:
65:protein domains
28:
23:
22:
15:
12:
11:
5:
5306:
5304:
5296:
5295:
5290:
5285:
5275:
5274:
5268:
5267:
5265:
5264:
5249:
5247:
5243:
5242:
5239:
5238:
5236:
5235:
5230:
5225:
5220:
5215:
5210:
5205:
5200:
5194:
5192:
5186:
5185:
5183:
5182:
5177:
5173:
5169:
5165:
5160:
5155:
5150:
5145:
5140:
5118:
5113:
5108:
5103:
5098:
5093:
5088:
5083:
5078:
5072:
5070:
5064:
5063:
5061:
5060:
5055:
5051:
5043:
5037:
5031:
5027:
5017:
5013:
5003:
4995:
4991:
4987:
4981:
4977:
4971:
4967:
4961:
4957:
4939:
4935:
4925:
4921:
4914:
4912:
4903:
4899:
4898:
4890:
4888:
4887:
4880:
4873:
4865:
4859:
4858:
4853:
4846:Metalloprotein
4841:
4840:External links
4838:
4836:
4835:
4820:
4794:
4765:
4739:
4724:
4698:
4683:
4657:
4628:
4602:
4573:
4547:
4518:
4492:
4485:
4467:
4438:
4412:
4379:
4353:
4320:
4294:
4271:
4245:
4230:
4204:
4189:
4163:
4128:
4093:
4058:
4019:(19): 5903–8.
3999:
3960:(7): 2056–61.
3940:
3905:
3846:
3817:(5): 1369–79.
3797:
3762:
3713:
3654:
3611:
3596:
3570:
3531:
3524:
3506:
3499:
3481:
3446:
3439:
3413:
3370:
3349:
3342:
3324:
3289:
3264:
3221:
3178:
3129:
3098:(7): 1769–73.
3078:
3069:|journal=
3051:
3025:
2976:
2969:
2951:
2944:
2926:
2911:
2904:
2886:
2863:
2859:
2837:
2814:
2805:
2786:(13): 3980–7.
2770:
2759:(3): 715–726.
2742:
2734:
2706:
2681:
2655:
2614:
2555:
2540:
2514:
2471:
2452:(2): 155–158.
2429:
2410:(11): 3173–8.
2394:
2382:
2375:
2354:
2339:
2312:
2310:
2307:
2305:
2304:
2299:
2294:
2289:
2284:
2279:
2274:
2269:
2264:
2259:
2254:
2249:
2243:
2241:
2238:
2235:
2234:
2225:
2221:
2220:
2215:
2209:
2208:
2206:DMSO reductase
2191:
2185:
2184:
2174:
2168:
2167:
2161:Aminopeptidase
2150:
2144:
2143:
2126:
2120:
2119:
2105:
2099:
2098:
2081:
2075:
2074:
2057:
2051:
2050:
2041:
2035:
2034:
2029:
2023:
2022:
2015:DNA polymerase
2004:
1998:
1997:
1994:
1966:
1963:
1922:
1919:
1887:
1884:
1822:
1819:
1817:
1814:
1794:Deoxyribozymes
1764:Group I intron
1746:
1743:
1734:
1733:
1729:
1721:
1714:
1713:
1709:
1701:
1689:
1679:Main article:
1676:
1673:
1628:enclosed in a
1622:photosynthesis
1576:
1573:
1568:
1563:) ligands, to
1560:
1556:
1552:
1548:
1509:
1508:
1504:
1500:
1493:
1485:
1482:
1475:
1451:
1450:
1447:
1443:
1439:
1432:
1387:microorganisms
1355:
1334:
1331:
1326:
1322:
1314:
1310:
1302:
1299:
1298:
1295:
1291:
1282:
1272:
1220:
1217:
1205:organometallic
1172:
1160:
1151:
1141:
1137:
1134:
1128:at biological
1122:
1121:
1114:
1105:
1101:
1066:
1065:
1058:
1048:
1037:
1036:
1033:
1029:
1025:
1021:
1011:carbon dioxide
978:
975:
947:
946:Metalloenzymes
944:
936:Main article:
933:
930:
914:Main article:
911:
908:
864:
861:
859:
856:
838:
816:
812:
800:
796:
788:
784:
780:
776:
772:
738:Main article:
735:
732:
706:-metabolizing
693:Main article:
679:
676:
634:metalloenzymes
595:Main article:
592:
589:
573:erythrocruorin
559:
547:horseshoe crab
524:
452:
427:molecule or a
415:(PIX) and the
395:
392:
387:
384:
369:
357:and the amide
341:residues, and
306:
303:
300:
299:
296:
293:
290:
287:
284:
281:
273:
272:
269:
266:
263:
260:
257:
254:
246:
245:
242:
239:
236:
233:
230:
227:
219:
218:
215:
212:
209:
206:
203:
200:
192:
191:
188:
185:
182:
179:
176:
173:
165:
164:
161:
158:
155:
152:
149:
146:
138:
137:
134:
131:
128:
125:
122:
119:
72:
69:
53:Metalloprotein
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
5305:
5294:
5291:
5289:
5286:
5284:
5281:
5280:
5278:
5263:
5262:
5256:
5255:
5251:
5250:
5248:
5244:
5234:
5231:
5229:
5226:
5224:
5221:
5219:
5216:
5214:
5211:
5209:
5206:
5204:
5201:
5199:
5196:
5195:
5193:
5191:
5187:
5181:
5174:
5172:
5166:
5164:
5161:
5159:
5156:
5154:
5153:Molybdopterin
5151:
5149:
5146:
5144:
5141:
5138:
5134:
5130:
5126:
5122:
5119:
5117:
5114:
5112:
5109:
5107:
5106:Cofactor F430
5104:
5102:
5099:
5097:
5094:
5092:
5089:
5087:
5084:
5082:
5079:
5077:
5074:
5073:
5071:
5069:
5065:
5059:
5058:Coenzyme F420
5056:
5049:
5041:
5040:Phylloquinone
5038:
5035:
5034:Ascorbic acid
5032:
5025:
5021:
5018:
5011:
5007:
4999:
4992:
4985:
4982:
4975:
4972:
4965:
4962:
4955:
4951:
4947:
4943:
4940:
4933:
4929:
4926:
4919:
4916:
4915:
4913:
4911:
4907:
4904:
4900:
4896:
4893:
4886:
4881:
4879:
4874:
4872:
4867:
4866:
4863:
4857:
4854:
4851:
4847:
4844:
4843:
4839:
4831:
4827:
4823:
4817:
4813:
4809:
4805:
4798:
4795:
4790:
4784:
4776:
4772:
4768:
4762:
4758:
4754:
4750:
4743:
4740:
4735:
4731:
4727:
4721:
4717:
4713:
4709:
4702:
4699:
4694:
4690:
4686:
4680:
4676:
4672:
4668:
4661:
4658:
4653:
4647:
4639:
4635:
4631:
4625:
4621:
4617:
4613:
4606:
4603:
4598:
4592:
4584:
4580:
4576:
4570:
4566:
4562:
4558:
4551:
4548:
4543:
4537:
4529:
4525:
4521:
4515:
4511:
4507:
4503:
4496:
4493:
4488:
4482:
4478:
4471:
4468:
4463:
4457:
4449:
4445:
4441:
4435:
4431:
4427:
4423:
4416:
4413:
4408:
4404:
4399:
4394:
4390:
4386:
4382:
4376:
4372:
4368:
4364:
4357:
4354:
4349:
4345:
4340:
4335:
4331:
4327:
4323:
4317:
4313:
4309:
4305:
4298:
4295:
4290:
4286:
4282:
4278:
4274:
4268:
4264:
4260:
4256:
4249:
4246:
4241:
4237:
4233:
4231:9783110434330
4227:
4223:
4219:
4215:
4208:
4205:
4200:
4196:
4192:
4186:
4182:
4178:
4174:
4167:
4164:
4159:
4155:
4151:
4147:
4144:(1): 405–21.
4143:
4139:
4132:
4129:
4124:
4120:
4116:
4112:
4108:
4104:
4097:
4094:
4089:
4085:
4081:
4077:
4074:(8): 906–10.
4073:
4069:
4062:
4059:
4054:
4050:
4045:
4040:
4035:
4030:
4026:
4022:
4018:
4014:
4010:
4003:
4000:
3995:
3991:
3986:
3981:
3976:
3971:
3967:
3963:
3959:
3955:
3951:
3944:
3941:
3936:
3932:
3928:
3924:
3920:
3916:
3909:
3906:
3901:
3897:
3892:
3887:
3882:
3877:
3873:
3869:
3866:(9): 4262–6.
3865:
3861:
3857:
3850:
3847:
3842:
3838:
3833:
3828:
3824:
3820:
3816:
3812:
3808:
3801:
3798:
3793:
3789:
3785:
3781:
3777:
3773:
3766:
3763:
3758:
3754:
3749:
3744:
3740:
3736:
3733:(8): 606–10.
3732:
3728:
3724:
3717:
3714:
3709:
3705:
3700:
3695:
3690:
3685:
3681:
3677:
3673:
3669:
3665:
3658:
3655:
3650:
3646:
3642:
3638:
3634:
3630:
3626:
3622:
3615:
3612:
3607:
3603:
3599:
3593:
3589:
3585:
3581:
3574:
3571:
3566:
3562:
3558:
3554:
3550:
3546:
3542:
3535:
3532:
3527:
3521:
3517:
3510:
3507:
3502:
3496:
3492:
3485:
3482:
3477:
3473:
3469:
3465:
3461:
3457:
3450:
3447:
3442:
3440:9780841227088
3436:
3432:
3427:
3426:
3417:
3414:
3409:
3405:
3401:
3397:
3393:
3389:
3385:
3381:
3374:
3371:
3359:
3353:
3350:
3345:
3339:
3335:
3328:
3325:
3320:
3316:
3312:
3308:
3304:
3300:
3293:
3290:
3279:on 2017-03-26
3278:
3274:
3268:
3265:
3260:
3256:
3252:
3248:
3244:
3240:
3236:
3232:
3225:
3222:
3217:
3213:
3209:
3205:
3201:
3197:
3193:
3189:
3182:
3179:
3174:
3170:
3165:
3160:
3156:
3152:
3148:
3144:
3140:
3133:
3130:
3125:
3121:
3116:
3111:
3106:
3101:
3097:
3093:
3089:
3082:
3079:
3074:
3062:
3054:
3048:
3044:
3040:
3036:
3029:
3026:
3021:
3017:
3013:
3009:
3005:
3001:
2997:
2993:
2992:
2987:
2980:
2977:
2972:
2966:
2962:
2955:
2952:
2947:
2941:
2937:
2930:
2927:
2922:
2915:
2912:
2907:
2901:
2897:
2890:
2887:
2882:
2878:
2874:
2871:
2870:
2857:
2853:
2849:
2841:
2838:
2833:
2829:
2825:
2822:
2821:
2809:
2806:
2801:
2797:
2793:
2789:
2785:
2781:
2774:
2771:
2766:
2762:
2758:
2755:
2754:
2746:
2743:
2737:
2731:
2727:
2723:
2719:
2713:
2711:
2707:
2702:
2698:
2693:
2688:
2684:
2682:9783110434330
2678:
2674:
2670:
2666:
2659:
2656:
2651:
2647:
2642:
2637:
2634:(2): 117–25.
2633:
2629:
2625:
2618:
2615:
2610:
2606:
2601:
2596:
2591:
2586:
2582:
2578:
2574:
2570:
2566:
2559:
2556:
2551:
2547:
2543:
2537:
2533:
2529:
2525:
2518:
2515:
2510:
2506:
2502:
2498:
2494:
2490:
2486:
2482:
2475:
2472:
2467:
2463:
2459:
2455:
2451:
2447:
2440:
2433:
2430:
2425:
2421:
2417:
2413:
2409:
2405:
2398:
2395:
2391:
2386:
2383:
2378:
2372:
2368:
2361:
2359:
2355:
2350:
2346:
2342:
2336:
2332:
2328:
2324:
2317:
2314:
2308:
2303:
2300:
2298:
2295:
2293:
2290:
2288:
2285:
2283:
2282:Deoxyribozyme
2280:
2278:
2275:
2273:
2270:
2268:
2265:
2263:
2260:
2258:
2255:
2253:
2250:
2248:
2245:
2244:
2239:
2233:
2229:
2226:
2223:
2222:
2219:
2216:
2214:
2211:
2210:
2207:
2203:
2199:
2195:
2192:
2190:
2187:
2186:
2182:
2178:
2175:
2173:
2170:
2169:
2166:
2162:
2158:
2154:
2151:
2149:
2146:
2145:
2142:
2138:
2134:
2130:
2127:
2125:
2122:
2121:
2117:
2113:
2109:
2106:
2104:
2101:
2100:
2097:
2093:
2089:
2085:
2082:
2080:
2077:
2076:
2073:
2069:
2065:
2061:
2058:
2056:
2053:
2052:
2049:
2045:
2042:
2040:
2037:
2036:
2033:
2030:
2028:
2025:
2024:
2021:
2020:
2016:
2012:
2008:
2005:
2003:
2000:
1999:
1995:
1992:
1991:
1988:
1985:
1983:
1979:
1974:
1972:
1964:
1962:
1959:
1955:
1951:
1943:
1939:
1935:
1931:
1927:
1920:
1918:
1916:
1912:
1909:, along with
1908:
1904:
1903:concentration
1901:
1897:
1893:
1885:
1883:
1881:
1876:
1874:
1870:
1866:
1862:
1858:
1857:aspartic acid
1854:
1853:glutamic acid
1850:
1845:
1843:
1839:
1835:
1829:EF-hand motif
1827:
1820:
1815:
1813:
1811:
1807:
1803:
1799:
1795:
1791:
1789:
1785:
1781:
1777:
1773:
1769:
1765:
1760:
1759:Sidney Altman
1756:
1752:
1744:
1738:
1727:
1726:
1725:
1720:cleavage of H
1719:
1707:
1706:
1705:
1699:
1696:
1692:
1682:
1674:
1672:
1670:
1666:
1662:
1658:
1657:triplet state
1654:
1651:undergoes an
1650:
1649:excited state
1646:
1645:singlet state
1642:
1637:
1635:
1631:
1627:
1623:
1615:
1611:
1607:
1603:
1599:
1595:
1591:
1586:
1582:
1574:
1572:
1566:
1546:
1545:square planar
1542:
1538:
1534:
1530:
1526:
1522:
1518:
1517:tetrahedrally
1514:
1486:
1468:
1467:
1466:
1464:
1460:
1456:
1425:
1424:
1423:
1421:
1417:
1413:
1399:
1394:
1392:
1388:
1384:
1380:
1376:
1372:
1368:
1364:
1348:
1339:
1332:
1330:
1320:
1308:
1289:
1285:
1278:
1270:
1269:
1268:
1266:
1262:
1258:
1255:
1251:
1247:
1243:
1240:
1239:
1234:
1230:
1226:
1218:
1216:
1214:
1210:
1206:
1202:
1198:
1194:
1190:
1186:
1182:
1178:
1170:
1166:
1158:
1154:
1147:
1135:
1133:
1131:
1127:
1126:carbonic acid
1099:
1098:
1097:
1095:
1091:
1087:
1083:
1079:
1075:
1071:
1064:
1046:
1045:
1044:
1042:
1019:
1018:
1017:
1016:
1015:carbonic acid
1012:
1008:
1000:
996:
992:
988:
983:
976:
974:
972:
968:
964:
960:
956:
953:
945:
943:
939:
931:
929:
927:
923:
917:
916:Ceruloplasmin
909:
907:
905:
901:
897:
896:iron overload
893:
889:
888:aspartic acid
885:
881:
877:
873:
869:
862:
857:
855:
853:
849:
845:
841:
837:
831:
826:
823:
819:
810:
806:
794:
770:
766:
762:
758:
751:
746:
741:
733:
731:
729:
725:
721:
717:
713:
709:
705:
701:
696:
688:
684:
677:
675:
673:
669:
667:
666:mitochondrial
663:
659:
655:
651:
647:
643:
639:
635:
631:
627:
623:
619:
615:
611:
607:
603:
598:
590:
588:
586:
582:
578:
574:
570:
569:Chlorocruorin
566:
552:
548:
544:
540:
536:
532:
530:
522:
518:
514:
510:
506:
502:
500:
496:
492:
489:
485:
484:oxyhemoglobin
481:
477:
473:
469:
464:
462:
458:
450:
446:
442:
438:
434:
430:
426:
422:
418:
414:
411:
408:
404:
400:
393:
391:
385:
383:
381:
377:
374:
367:
362:
360:
356:
352:
348:
344:
340:
336:
332:
328:
324:
320:
316:
312:
304:
297:
294:
291:
288:
285:
282:
279:
275:
274:
270:
267:
264:
261:
258:
255:
252:
248:
247:
243:
240:
237:
234:
231:
228:
225:
221:
220:
216:
213:
210:
207:
204:
201:
198:
194:
193:
189:
186:
183:
180:
177:
174:
171:
167:
166:
162:
159:
156:
153:
150:
147:
144:
140:
139:
135:
132:
129:
126:
123:
120:
118:
117:
111:
109:
105:
102:
97:
94:
90:
86:
82:
78:
70:
68:
66:
62:
58:
54:
47:
43:
39:
34:
30:
19:
18:Metalloenzyme
5258:
5252:
5158:Mycofactocin
5148:Methanofuran
5068:non-vitamins
4902:Active forms
4803:
4797:
4748:
4742:
4707:
4701:
4666:
4660:
4611:
4605:
4556:
4550:
4501:
4495:
4476:
4470:
4421:
4415:
4362:
4356:
4303:
4297:
4254:
4248:
4213:
4207:
4172:
4166:
4141:
4137:
4131:
4109:(8): 322–8.
4106:
4102:
4096:
4071:
4067:
4061:
4016:
4012:
4002:
3957:
3953:
3943:
3921:(4): 223–9.
3918:
3914:
3908:
3863:
3859:
3849:
3814:
3810:
3800:
3778:(4): 223–9.
3775:
3771:
3765:
3730:
3726:
3716:
3671:
3667:
3657:
3624:
3620:
3614:
3579:
3573:
3548:
3545:Biochemistry
3544:
3534:
3515:
3509:
3490:
3484:
3459:
3455:
3449:
3424:
3416:
3383:
3379:
3373:
3362:. Retrieved
3352:
3333:
3327:
3302:
3298:
3292:
3281:. Retrieved
3277:the original
3267:
3237:(3): 215–9.
3234:
3230:
3224:
3194:(4): 200–9.
3191:
3187:
3181:
3149:(2): 51–62.
3146:
3142:
3132:
3095:
3091:
3081:
3034:
3028:
2995:
2989:
2979:
2960:
2954:
2935:
2929:
2920:
2914:
2895:
2889:
2872:
2867:
2855:
2851:
2847:
2840:
2823:
2818:
2808:
2783:
2779:
2773:
2756:
2751:
2745:
2721:
2664:
2658:
2631:
2627:
2617:
2572:
2568:
2558:
2523:
2517:
2487:(1): 25–35.
2484:
2480:
2474:
2449:
2445:
2432:
2407:
2403:
2397:
2385:
2366:
2322:
2316:
2272:Hemoproteins
2165:Beta amyloid
2017:
1986:
1975:
1968:
1947:
1889:
1877:
1846:
1832:
1812:-specific).
1792:
1748:
1715:
1684:
1665:free radical
1638:
1619:
1535:may contain
1510:
1452:
1395:
1371:free radical
1344:
1300:
1286:+ 16 Mg
1275:+ 16 Mg
1237:
1233:nitrogenases
1222:
1208:
1148:-containing
1143:
1123:
1090:nucleophilic
1067:
1038:
1004:
955:coordination
949:
941:
926:blood plasma
919:
866:
835:
827:
821:
817:
754:
750:plastocyanin
740:Plastocyanin
734:Plastocyanin
698:
689:active site.
670:
600:
577:blood plasma
567:
545:such as the
533:
503:
499:ionic radius
497:and smaller
488:paramagnetic
465:
437:muscle cells
397:
389:
363:
308:
98:
74:
52:
51:
29:
5143:Lipoic Acid
5121:Heme / Haem
5048:Menaquinone
3305:(1): 1–20.
2984:Colman PM,
2628:Metallomics
2287:Siderophore
2267:Dioxygenase
2232:Phosphatase
2112:Hydrogenase
2064:Hydrogenase
1954:zinc finger
1930:Zinc finger
1915:tropomyosin
1755:Thomas Cech
1718:heterolytic
1700:, driving H
1681:Hydrogenase
1675:Hydrogenase
1669:chloroplast
1598:chlorophyll
1596:(left) and
1585:photosystem
1581:chlorophyll
1455:dismutation
1396:The formal
1229:triple bond
1094:equilibrium
1086:tetrahedral
963:active site
938:Osteopontin
904:thalassemia
880:transferrin
844:Protonation
795:) than Cu−S
720:tetrahedron
646:amino acids
626:cytochromes
591:Cytochromes
585:polychaetes
541:, and some
535:Hemocyanins
509:carboxylate
505:Hemerythrin
476:diamagnetic
441:hydrophobic
435:, found in
407:macrocyclic
373:macrocyclic
343:carboxylate
5277:Categories
5246:Base forms
5190:metal ions
5116:Coenzyme Q
5111:Coenzyme M
5101:Coenzyme B
4964:Coenzyme A
4918:TPP / ThDP
3541:Getzoff ED
3364:2008-10-06
3283:2017-03-24
2986:Freeman HC
2753:Chem. Rev.
2309:References
2189:Molybdenum
2011:Hexokinase
1978:calmodulin
1834:Calmodulin
1821:Calmodulin
1776:hammerhead
1594:Hemoglobin
1383:phagocytes
1347:superoxide
1290:+16 P
1246:molybdenum
1197:sigma bond
876:hydrolysis
700:Rubredoxin
687:Rubredoxin
678:Rubredoxin
597:cytochrome
543:arthropods
482:state. In
468:hemoglobin
399:Hemoglobin
333:residues,
323:amino acid
108:hemoglobin
79:contain a
38:hemoglobin
5176:THMPT / H
4974:PLP / P5P
4895:cofactors
4783:cite book
4775:1868-0402
4646:cite book
4638:1868-0402
4591:cite book
4583:1868-0402
4536:cite book
4528:1868-0402
4456:cite book
4448:1868-0402
4389:1868-0402
4330:1868-0402
4281:1868-0402
3155:0159-8090
3071:ignored (
3061:cite book
2898:. Wiley.
2302:QPNC-PAGE
2183:proteins
2072:Aconitase
2039:Manganese
2002:Magnesium
1944:residues.
1938:histidine
1861:bidentate
1751:ribozymes
1698:catalysts
1626:magnesium
1602:magnesium
1531:). Other
1521:histidine
1438:+ 2 H → O
1307:phosphate
1254:magnesium
1238:Rhizobium
1201:adenosine
1193:imidazole
1165:C−C bonds
1150:Vitamin B
1136:Vitamin B
1082:histidine
1078:imidazole
1041:hydroxide
995:hydroxide
991:histidine
967:catalyzes
892:histidine
884:tyrosines
728:high spin
644:found in
614:oxidizing
606:reduction
602:Oxidation
521:histidine
519:and five
517:aspartate
513:glutamate
472:myoglobin
433:myoglobin
421:histidine
417:imidazole
366:cofactors
347:aspartate
331:histidine
327:imidazole
232:<5-12
202:<2-13
163:<4-40
143:manganese
71:Abundance
5261:vitamins
5254:vitamins
5168:THB / BH
5002:DHFA / H
4994:THFA / H
4910:vitamins
4830:25416389
4734:23430778
4693:23430777
4407:23595675
4348:23595673
4289:23595671
4240:28731300
4199:25416390
4123:10884684
4053:25918425
3994:17284609
3841:25939889
3757:26167874
3708:10535916
3606:25416392
3565:15209499
3408:95235740
3173:28303071
2800:12656634
2701:28731303
2650:21069142
2609:30634485
2575:(8): 8.
2550:24470087
2501:19079350
2424:17081069
2349:23595668
2262:Coenzyme
2257:Biometal
2240:See also
2213:Tungsten
2181:Thiolate
2060:Catalase
2044:Arginase
2032:vanabins
2027:Vanadium
1942:cysteine
1907:Troponin
1890:In both
1886:Troponin
1641:electron
1533:isozymes
1519:by four
1367:electron
1242:bacteria
1177:coenzyme
1132:values.
1001:in gray.
890:and one
872:ferritin
842:of 4.4.
716:cysteine
708:bacteria
581:annelids
579:of many
539:mollusks
529:peroxide
480:low-spin
466:In both
445:oxidized
429:dioxygen
359:carbonyl
351:proteome
339:cysteine
335:thiolate
311:nitrogen
217:150 (?)
208:<2-8
77:proteins
61:cofactor
4398:3924584
4339:6542352
4158:2114117
4088:6313166
4044:4434688
4021:Bibcode
3985:1892917
3962:Bibcode
3935:9383394
3900:9113977
3868:Bibcode
3832:4439366
3792:9383394
3748:4509812
3676:Bibcode
3649:7688142
3629:Bibcode
3621:Science
3476:8484118
3456:Science
3388:Bibcode
3319:9336012
3259:7925719
3251:3738220
3216:8808191
3196:Bibcode
3164:5198508
3124:3470756
3020:4226644
3000:Bibcode
2692:5771651
2600:6463171
2577:Bibcode
2509:7253420
2466:9667942
2224:various
2172:Cadmium
2133:Laccase
1900:calcium
1892:cardiac
1865:glycine
1849:EF-hand
1838:EF-hand
1780:hairpin
1772:RNase P
1732:⇌ H + H
1630:chlorin
1559:and Cys
1551:and Cys
1481:→ M + O
1426:2
1405:⁄
1319:cubical
1301:where P
1051:+ OH ⇌
959:enzymes
932:Calcium
712:archaea
376:ligands
271:85-305
244:<15
181:24,967
175:16,769
136:Muscle
124:Kidney
89:enzymes
57:protein
5208:Fe, Fe
5020:AdoCbl
4984:Biotin
4892:Enzyme
4852:(MeSH)
4828:
4818:
4773:
4763:
4732:
4722:
4691:
4681:
4636:
4626:
4581:
4571:
4526:
4516:
4483:
4446:
4436:
4405:
4395:
4387:
4377:
4346:
4336:
4328:
4318:
4287:
4279:
4269:
4238:
4228:
4197:
4187:
4156:
4121:
4086:
4051:
4041:
3992:
3982:
3933:
3898:
3888:
3839:
3829:
3790:
3755:
3745:
3706:
3696:
3647:
3604:
3594:
3563:
3522:
3497:
3474:
3437:
3406:
3340:
3317:
3257:
3249:
3214:
3171:
3161:
3153:
3122:
3115:304522
3112:
3049:
3018:
2991:Nature
2967:
2942:
2902:
2798:
2732:
2699:
2689:
2679:
2648:
2607:
2597:
2548:
2538:
2507:
2499:
2464:
2422:
2373:
2347:
2337:
2124:Copper
2118:(MCR)
2108:Urease
2103:Nickel
2079:Cobalt
2068:IRE-BP
1932:. The
1847:In an
1810:sodium
1806:uranyl
1802:copper
1786:, and
1634:photon
1541:nickel
1513:copper
1363:oxygen
1265:legume
1189:corrin
1157:methyl
1146:cobalt
1013:forms
952:labile
922:copper
910:Copper
886:, one
848:ligand
765:copper
704:sulfur
658:heme b
654:heme a
551:copper
410:ligand
355:amides
319:sulfur
315:oxygen
298:4,688
292:2,772
289:1,470
286:5,018
283:5,543
251:copper
241:<5
238:<5
235:<5
229:<5
224:nickel
214:<2
205:<2
197:cobalt
190:3,500
187:4,100
184:5,530
178:7,168
133:Brain
130:Heart
121:Liver
40:. The
5024:MeCbl
4954:NADPH
3891:20710
3699:22911
3404:S2CID
3255:S2CID
3016:S2CID
2505:S2CID
2442:(PDF)
1948:Many
1911:actin
1844:ion.
1695:redox
1379:toxic
1349:ion,
1209:trans
1028:O ⇌ H
775:and N
461:lungs
425:water
127:Lung
101:human
85:cells
81:metal
5259:see
5091:PAPS
5086:SAMe
5010:MTHF
4950:NADP
4946:NADH
4826:PMID
4816:ISBN
4789:link
4771:ISSN
4761:ISBN
4730:PMID
4720:ISBN
4689:PMID
4679:ISBN
4652:link
4634:ISSN
4624:ISBN
4597:link
4579:ISSN
4569:ISBN
4542:link
4524:ISSN
4514:ISBN
4481:ISBN
4462:link
4444:ISSN
4434:ISBN
4403:PMID
4385:ISSN
4375:ISBN
4344:PMID
4326:ISSN
4316:ISBN
4285:PMID
4277:ISSN
4267:ISBN
4236:PMID
4226:ISBN
4195:PMID
4185:ISBN
4154:PMID
4119:PMID
4084:PMID
4049:PMID
3990:PMID
3931:PMID
3896:PMID
3837:PMID
3788:PMID
3753:PMID
3704:PMID
3645:PMID
3602:PMID
3592:ISBN
3561:PMID
3520:ISBN
3495:ISBN
3472:PMID
3435:ISBN
3338:ISBN
3315:PMID
3247:PMID
3212:PMID
3169:PMID
3151:ISSN
3120:PMID
3073:help
3047:ISBN
2965:ISBN
2940:ISBN
2900:ISBN
2796:PMID
2730:ISBN
2697:PMID
2677:ISBN
2646:PMID
2605:PMID
2569:Life
2546:PMID
2536:ISBN
2497:PMID
2462:PMID
2420:PMID
2371:ISBN
2345:PMID
2335:ISBN
2148:Zinc
2055:Iron
1934:zinc
1913:and
1894:and
1873:hard
1855:and
1798:lead
1757:and
1661:spin
1606:iron
1583:and
1537:iron
1525:zinc
1345:The
1223:The
1159:(−CH
1144:The
1074:zinc
1043:ion
999:zinc
868:Iron
863:Iron
710:and
650:heme
622:Iron
604:and
515:and
470:and
403:iron
380:heme
295:915
278:zinc
276:Zn (
268:401
265:350
262:220
259:379
256:882
249:Cu (
222:Ni (
211:---
195:Co (
170:iron
168:Fe (
148:138
141:Mn (
104:body
91:and
46:iron
42:heme
5180:MPT
5163:PQQ
5096:GSH
5081:CTP
5076:ATP
5046:),
5036:(C)
4942:NAD
4932:FAD
4928:FMN
4808:doi
4753:doi
4712:doi
4671:doi
4616:doi
4561:doi
4506:doi
4426:doi
4393:PMC
4367:doi
4334:PMC
4308:doi
4259:doi
4218:doi
4177:doi
4146:doi
4111:doi
4076:doi
4039:PMC
4029:doi
4017:112
3980:PMC
3970:doi
3958:104
3923:doi
3886:PMC
3876:doi
3827:PMC
3819:doi
3780:doi
3743:PMC
3735:doi
3694:PMC
3684:doi
3637:doi
3625:261
3584:doi
3553:doi
3464:doi
3460:260
3431:257
3396:doi
3384:288
3307:doi
3239:doi
3235:186
3204:doi
3159:PMC
3110:PMC
3100:doi
3039:doi
3008:doi
2996:272
2877:doi
2873:114
2828:doi
2824:109
2788:doi
2784:125
2761:doi
2687:PMC
2669:doi
2636:doi
2595:PMC
2585:doi
2528:doi
2489:doi
2454:doi
2412:doi
2327:doi
1993:Ion
1958:DNA
1784:HDV
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