477:, which is 5 x 10 M.sec compared to the blue copper protein which is between 1ms and 01ÎĽs. Upon electron transfer the oxidized Cu state at the blue copper protein active site will be minimized because the Jahn-Teller effect is minimized. The distorted geometry prevents Jahn-Teller distortion. The orbital degeneracy is removed due to the asymmetric ligand field. The asymmetric ligand field is influenced by the strong equatorial cysteine ligand and the weak axial methionine ligand. In Figure 2, an energy level diagram shows three different relevant geometries and their d-orbital splitting and the Jahn-Teller effect is shown in blue. (i) shows the tetrahedral geometry energy level diagram with a that is degenerate. The tetrahedral structure can undergo Jahn-Teller distortion because of the degenerate orbitals. (ii) shows the C
274:”, which means a protein can perform more than one function. They serve as electron transfer agents, with the active site shuttling between Cu(I) and Cu(II). The Cu in the oxidized state can accept one electron to form Cu in the reduced protein. The geometry of the Cu center has a major impact on its redox properties. The Jahn-Teller distortion does not apply to the blue copper proteins because the copper site has low symmetry that does not support degeneracy in the d-orbital manifold. The absence of large reorganizational changes enhances the rate of their electron transfer. The active site of a type-I blue copper protein. Two 2-histidines, 1 methionine and 1 cysteine present in the coordination sphere. Example for Type-I blue copper protein are
322:
461:
388:
showed that both bands have the same polarization ratio that associated with Cu(II)-S(Cys) bond. This is explained that the normal cupric complex has high energy intense sigma and low energy weak π bonds. However, in the blue copper protein case have low energy intense sigma and high energy weak π
490:
geometry with a longer thioester bond and a subsequently shorter thiolate bond. This is the proper geometry of the blue copper protein. This shows that there is no presence of the Jahn-Teller effect. The energy diagram shows that the asymmetry of the short Cu-S(Cys) bond and the highly distorted
374:
will be formed due to the strong equatorial cysteine ligand and the weak axial methionine ligand. The two neutral histidine ligands are positioned by the protein ligand so the geometry is distorted tetrahedral. This will cause them not to be able to coordinate perfectly as tetrahedral or a square
341:
as they also identify as Type 1 copper proteins. They are also similar to one another due to the geometry of the copper site of each copper protein. The protein azurin has a trigonal bipyramidal geometry with elongated axial glycine and methoinione sulfur ligands. Plastocyanins have an additional
383:
Lowering the temperature may change the transitions. The intense absorbance at about 16000 cm was characterized the absorptions feature of blue copper. There was a second lower energy feature band with moderate absorption intensity. Polarized signal-crystal absorption data on
181:
consist of a pair of copper centres, each coordinated by three histidine residues. These proteins exhibit no EPR signal due to strong antiferromagnetic coupling (i.e. spin pairing) between the two S = 1/2 metal ions due to their covalent overlap with a
144:), which usually gives rise to a blue colour. Cupredoxins are therefore often called "blue copper proteins". This may be misleading, since some T1Cu centres also absorb around 460 nm and are therefore green. When studied by
132:
residue). T1Cu-containing proteins are usually called "cupredoxins", and show similar three-dimensional structures, relatively high reduction potentials (> 250 mV), and strong absorption near 600 nm (due to
170:
in the parallel region similar to that observed in regular copper coordination compounds. Since no sulfur ligation is present, the optical spectra of these centres lack distinctive features. T2Cu centres occur in
636:
Arcos-LĂłpez, Trinidad; Schuth, Nils; Quintanar, Liliana (2020), "Chapter 3: The Type 1 Blue Copper Site: From
Electron Transfer to Biological Function", in Sosa Torres, Martha E.; Kroneck, Peter M.H. (eds.),
485:
geometry was formed by the elongated methionine thioether bond at the reduced site. The unpaired electrons leads to the Jahn-Teller effect. (iii) shows the ground state energy level splitting diagram of the
491:
Cu-L bond angles causes the degeneracy of the orbitals to be removed and thereby removing the Jahn-Teller effect, which is due to the weak donor at an Cu-S(Met) and strong donor at Cu-S(Met).
342:
methionine sulfur ligand on the axial position. The main difference of each copper protein is that each protein has different number and species of ligand coordinated to the copper center.
350:
The strong bond between the copper ion and the cysteine sulfur allows for the non-bonded electron on the cysteine sulfur to be present on both the low/high spin state copper ion, d
397:
bond giving dominant π overlap with sulfur directly. Finally, the nature of the ground state wave function of the blue copper protein is rich in electron absorption spectrum.
549:
Członkowska, Anna; Litwin, Tomasz; Dusek, Petr; Ferenci, Peter; Lutsenko, Svetlana; Medici, Valentina; Rybakowski, Janusz K.; Weiss, Karl Heinz; Schilsky, Michael L. (2018).
101:
298:
The Blue Copper
Proteins, a class of Type 1 copper proteins, are small proteins containing a cupredoxin fold and a single Type I copper ion coordinated by two
409:, protein structures are still formed with elongated bonds by 0.1 Ă… or less. with the oxidized and reduced protein structures, they are superimposable. With
318:
to metal charge transfer an intense band at 600 nm that gives the characteristic of a deep blue colour present in the electron absorption spectrum.
314:
ion will form either a trigonal bipyramidal or tetrahedral coordination. The Type 1 copper proteins are identified as blue copper proteins due to the
148:
spectroscopy, T1Cu centres show small hyperfine splittings in the parallel region of the spectrum (compared to common copper coordination compounds).
228:). The two copper atoms are coordinated by two histidines, one methionine, a protein backbone carbonyl oxygen, and two bridging cysteine residues.
69:
used in defense against free radicals, peptidyl-α-monooxygenase for the production of hormones, and tyrosinase, which affects skin pigmentation.
1018:
787:
641:, Metal Ions in Life Sciences (Series editors Astrid Sigel, Eva Freisinger and Roland K.O. Sigel), vol. 20, Berlin/Boston: de Gruyter,
333:, is built from polypeptide folds that are commonly found in blue copper proteins β sandwich structure. The structure is very similar to
533:
257:
is found in nitrous-oxide reductase. The four copper atoms are coordinated by seven histidine residues and bridged by a sulfur atom.
187:
57:). Some organisms even use copper proteins to carry oxygen instead of iron proteins. A prominent copper protein in humans is in
460:
371:
389:
bonds because CT intensity reflects overlap of the donor and acceptor orbitals in the CT process. This required that the 3d
367:
124:
contain the third type of T1Cu centres: besides a methionine in one axial position, they contain a second axial ligand (a
1013:
661:
Klinman JP (November 1996). "Mechanisms
Whereby Mononuclear Copper Proteins Functionalize Organic Substrates".
222:
45:. Copper proteins are found in all forms of air-breathing life. These proteins are usually associated with
218:
163:
145:
363:
601:, Kennepohl P, Solomon EI (November 1996). "Structural and Functional Aspects of Metal Sites in Biology".
62:
271:
239:
210:
66:
58:
413:, there is an exception due to the histidine being ligated and it is not bound to copper iodide. In
167:
481:
symmetric geometry energy level splitting diagram with an E ground state that is degenerate. The C
811:
990:
955:
863:
783:
749:
732:
Solomon EI, Sundaram UM, Machonkin TE (November 1996). "Multicopper
Oxidases and Oxygenases".
714:
678:
618:
580:
529:
321:
46:
982:
945:
937:
901:
853:
845:
775:
741:
706:
670:
642:
610:
570:
562:
500:
406:
42:
892:
Solomon EI, Hadt RG (April 2011). "Recent advances in understanding blue copper proteins".
598:
405:
The cysteine sulfur copper (II) ion bonds range from 2.6 to 3.2 Ă…. With the reduced form,
267:
183:
93:
834:"Blue copper proteins: a comparative analysis of their molecular interaction properties"
950:
925:
858:
833:
575:
550:
986:
1007:
426:
155:
941:
815:
433:
46 donates a hydrogen bond to the carbonyl backbone of
Asparagine10. The Cysteine84
394:
246:. The copper atom is coordinated by three histidines in trigonal pyramidal geometry.
974:
505:
474:
438:
385:
334:
275:
109:
779:
141:
77:
The metal centers in the copper proteins can be classified into several types:
17:
905:
647:
566:
442:
422:
307:
287:
283:
195:
191:
113:
994:
473:
Cu complexes often have relatively slow transfer rates. An example is the Cu
430:
410:
359:
330:
299:
117:
105:
85:
959:
867:
753:
718:
682:
622:
584:
393:
orbital of the blue copper site be oriented such that its lobes bisect the
266:
The blue copper proteins owe their name to their intense blue coloration (
418:
303:
125:
89:
61:(cco). This enzyme cco mediates the controlled combustion that produces
34:
849:
225:
454:
450:
446:
346:
Electronic structure of the blue copper protein type I copper complexes
129:
745:
710:
674:
614:
770:
Malmström BG (1994). "Rack-induced bonding in blue-copper proteins".
697:
Lewis EA, Tolman WB (2004). "Reactivity of
Dioxygen-Copper Systems".
445:
38, and
Histidine37 interacts strongly with the carbonyl backbone of
414:
338:
315:
279:
172:
159:
138:
134:
121:
97:
50:
38:
926:"Inner- and outer-sphere metal coordination in blue copper proteins"
362:
of the cysteine sulfur. Most copper (II) complexes will exhibit the
421:
112 thiolate accepts the hydrogen bonds from the amide backbone of
311:
434:
27:
Proteins that contain one or more copper ions as prosthetic groups
832:
De Rienzo F, Gabdoulline RR, Menziani MC, Wade RC (August 2000).
924:
Warren JJ, Lancaster KM, Richards JH, Gray HB (October 2012).
84:
are characterized by a single copper atom coordinated by two
639:
Transition Metals and Sulfur: A Strong
Relationship for Life
325:
The structure of active site of type 1- blue copper protein.
294:
Structure of the Blue Copper
Proteins Type I Copper Centers
370:
complex geometry. With blue copper proteins, a distorted
808:
Biological inorganic chemistry: structure and reactivity
329:
The protein structure of a Type 1 blue copper protein,
464:
Ligand field splitting diagram for blue copper protein
366:
when the complex forms a tetragonal distortion of an
112:
and pseudoazurin) the axial ligand is the sulfur of
175:, where they assist in oxidations or oxygenations.
774:. Berlin Heidelberg: Springer. pp. 157–164.
449:33 and more weakly with the carbonyl backbone of
186:. These centres are present in some oxidases and
116:, whereas aminoacids other than methionine (e.g.
457:34, and the amide backbone of Phenylalanine35.
441:accepts a hydrogen bond from a amide backbone,
310:thioether S-donor. In the oxidized state, the
120:) give rise to class II T1Cu copper proteins.
975:"Coordination compounds in the entatic state"
8:
270:). The blue copper protein often called as “
949:
857:
646:
574:
401:Inner and outer sphere metal coordination
459:
320:
516:
65:. Other copper proteins include some
919:
917:
915:
887:
885:
883:
881:
879:
877:
827:
825:
7:
801:
799:
765:
763:
469:Blue Copper Protein "Entatic State"
49:with or without the involvement of
526:Copper Proteins and Copper Enzymes
25:
930:Journal of Inorganic Biochemistry
379:Spectral changes with temperature
96:structure, and a variable axial
942:10.1016/j.jinorgbio.2012.05.002
979:Coordination Chemistry Reviews
894:Coordination Chemistry Reviews
555:Nature Reviews Disease Primers
179:Type III copper centres (T3Cu)
1:
987:10.1016/s0010-8545(00)00265-4
152:Type II copper centres (T2Cu)
1019:Peripheral membrane proteins
780:10.1007/978-3-642-79502-2_12
528:. Vol. III. CRC Press.
188:oxygen-transporting proteins
82:Type I copper centres (T1Cu)
1035:
282:, and nitrite reductase,
973:Comba, Peter (May 2000).
906:10.1016/j.ccr.2010.12.008
648:10.1515/9783110589757-003
567:10.1038/s41572-018-0018-3
162:. They exhibit an axial
158:coordination by N or N/O
37:that contain one or more
806:Bertini I (2007-07-01).
306:thiolate S-donor and a
219:nitrous-oxide reductase
524:Lontie R, ed. (2018).
465:
326:
463:
324:
166:spectrum with copper
102:class I T1Cu proteins
67:superoxide dismutases
981:. 200–202: 217–245.
272:moonlighting protein
262:Blue copper proteins
232:Copper B centres (Cu
203:Copper A centres (Cu
59:cytochrome c oxidase
850:10.1110/ps.9.8.1439
372:tetrahedral complex
251:Copper Z centre (Cu
168:hyperfine splitting
466:
364:Jahn-Teller effect
327:
789:978-3-540-58830-6
746:10.1021/cr950046o
711:10.1021/cr020633r
675:10.1021/cr950047g
615:10.1021/cr9500390
47:electron-transfer
43:prosthetic groups
16:(Redirected from
1026:
999:
998:
970:
964:
963:
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910:
909:
900:(7–8): 774–789.
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772:EJB Reviews 1994
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758:
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740:(7): 2563–2606.
734:Chemical Reviews
729:
723:
722:
705:(2): 1047–1076.
699:Chemical Reviews
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686:
669:(7): 2541–2562.
663:Chemical Reviews
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651:
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627:
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609:(7): 2239–2314.
603:Chemical Reviews
595:
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551:"Wilson disease"
546:
540:
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501:Copper in health
358:orbital and the
21:
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1014:Copper proteins
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249:A tetranuclear
235:
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184:bridging ligand
142:charge transfer
94:trigonal planar
88:residues and a
75:
56:
31:Copper proteins
28:
23:
22:
18:Copper proteins
15:
12:
11:
5:
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1021:
1016:
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844:(8): 1439–54.
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126:carbonyl group
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427:Phenylalanine
424:
420:
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408:
400:
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376:
373:
369:
365:
361:
345:
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332:
323:
319:
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313:
309:
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293:
291:
289:
285:
281:
277:
276:plastocyanine
273:
269:
261:
256:
248:
245:
243:
238:are found in
237:
230:
227:
224:
220:
216:
214:
209:are found in
208:
200:
197:
193:
189:
185:
180:
177:
174:
169:
165:
161:
157:
156:square planar
153:
150:
147:
143:
140:
136:
131:
127:
123:
119:
115:
111:
107:
103:
99:
95:
92:residue in a
91:
87:
83:
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72:
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68:
64:
60:
52:
48:
44:
40:
36:
32:
19:
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692:
666:
662:
656:
638:
631:
606:
602:
593:
558:
554:
544:
525:
519:
506:Stellacyanin
475:aquo complex
472:
439:plastocyanin
404:
386:plastocyanin
382:
349:
335:plastocyanin
328:
302:N-donors, a
297:
265:
250:
241:
231:
212:
202:
178:
151:
110:plastocyanin
81:
76:
30:
29:
284:haemocyanin
240:cytochrome
211:cytochrome
1008:Categories
936:: 119–26.
512:References
443:Asparagine
423:Asparagine
368:octahedral
308:methionine
288:tyrosinase
201:Binuclear
196:tyrosinase
192:hemocyanin
154:exhibit a
114:methionine
995:0010-8545
561:(1): 21.
431:Histidine
429:114, and
411:amicyanin
395:Cu-S(Cys)
360:p-orbital
331:amicyanin
300:histidine
118:glutamine
106:amicyanin
86:histidine
960:22658756
868:10975566
816:93183803
754:11848837
719:14871149
683:11848836
623:11848828
585:30190489
495:See also
435:thiolate
425:47, and
419:Cysteine
375:planar.
304:cysteine
226:1.7.99.6
90:cysteine
41:ions as
35:proteins
951:3434318
859:2144732
599:Holm RH
576:6416051
455:Glycine
451:Leucine
447:Alanine
244:oxidase
215:oxidase
173:enzymes
160:ligands
130:glycine
122:Azurins
73:Classes
993:
958:
948:
866:
856:
814:
786:
752:
717:
681:
621:
583:
573:
532:
417:, the
415:azurin
391:(x-y )
339:azurin
316:ligand
280:azurin
268:Cu(II)
190:(e.g.
104:(e.g.
98:ligand
51:oxygen
39:copper
812:S2CID
128:of a
100:. In
991:ISSN
956:PMID
864:PMID
784:ISBN
750:PMID
715:PMID
679:PMID
619:PMID
581:PMID
530:ISBN
337:and
286:and
217:and
194:and
33:are
983:doi
946:PMC
938:doi
934:115
902:doi
898:255
854:PMC
846:doi
776:doi
742:doi
707:doi
703:104
671:doi
643:doi
611:doi
571:PMC
563:doi
453:5,
437:of
407:CuI
164:EPR
146:EPR
63:ATP
1010::
989:.
977:.
954:.
944:.
932:.
928:.
914:^
896:.
876:^
862:.
852:.
840:.
836:.
824:^
810:.
798:^
782:.
762:^
748:.
738:96
736:.
713:.
701:.
677:.
667:96
665:.
617:.
607:96
605:.
579:.
569:.
557:.
553:.
483:3v
479:3v
354:-d
312:Cu
290:.
278:,
223:EC
198:).
139:Cu
108:,
53:(O
997:.
985::
962:.
940::
908:.
904::
870:.
848::
842:9
818:.
792:.
778::
756:.
744::
721:.
709::
687:.
685:.
673::
645::
625:.
613::
587:.
565::
559:4
538:.
488:s
486:C
356:y
352:x
255:)
253:Z
242:c
236:)
234:B
221:(
213:c
207:)
205:A
137:→
135:S
55:2
20:)
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