631:. When the photon has been absorbed, the resulting high-energy electron is transferred to a nearby pheophytin molecule. This is above and to the right of the pair on the diagram and is coloured grey. The electron travels from the pheophytin molecule through two plastoquinone molecules, the first tightly bound, the second loosely bound. The tightly bound molecule is shown above the pheophytin molecule and is colored red. The loosely bound molecule is to the left of this and is also colored red. This flow of electrons is similar to that of the bacterial reaction center. Two electrons are required to fully reduce the loosely bound plastoquinone molecule to QH
511:. Ingenhousz took green plants and immersed them in water inside a transparent tank. He observed many bubbles rising from the surface of the leaves whenever the plants were exposed to light. Ingenhousz collected the gas that was given off by the plants and performed several different tests in attempt to determine what the gas was. The test that finally revealed the identity of the gas was placing a smouldering taper into the gas sample and having it relight. This test proved it was oxygen, or, as Joseph Priestley had called it, 'de-
294:
364:), and a ferrous ion are associated with the L and M subunits. The H subunit, shown in gold, lies on the cytoplasmic side of the plasma membrane. A cytochrome subunit, not shown here, contains four c-type hemes and is located on the periplasmic surface (outer) of the membrane. The latter sub-unit is not a general structural motif in photosynthetic bacteria. The L and M subunits bind the functional and light-interacting cofactors, shown here in green.
535:
381:
612:
526:. Their experiment proved the existence of a photosynthetic unit. Gaffron and Wohl later interpreted the experiment and realized that the light absorbed by the photosynthetic unit was transferred. This reaction occurs at the reaction center of Photosystem II and takes place in cyanobacteria, algae and green plants.
718:
at which the chlorophyll molecules absorb light maximally. The P700 lies in the center of the protein. Once photoinduced charge separation has been initiated, the electron travels down a pathway through a chlorophyll α molecule situated directly above the P700, through a quinone molecule situated
670:
residue. Manganese is adept at these reactions because it is capable of existing in four oxidation states: Mn, Mn, Mn and Mn. Manganese also forms strong bonds with oxygen-containing molecules such as water. The process of oxidizing two molecules of water to form an oxygen molecule requires four
499:
in the confined space of the burning candle. He found that the mouse died a short time after the candle had been extinguished. However, he could revivify the foul air by placing green plants in the area and exposing them to light. Priestley's observations were some of the first experiments that
367:
Reaction centers from different bacterial species may contain slightly altered bacterio-chlorophyll and bacterio-pheophytin chromophores as functional co-factors. These alterations cause shifts in the colour of light that can be absorbed. The reaction center contains two pigments that serve to
545:
is the photosystem that generates the two electrons that will eventually reduce NADP in ferredoxin-NADP-reductase. Photosystem II is present on the thylakoid membranes inside chloroplasts, the site of photosynthesis in green plants. The structure of
Photosystem II is remarkably similar to the
553:. These two subunits are similar to the L and M subunits present in the bacterial reaction center. Photosystem II differs from the bacterial reaction center in that it has many additional subunits that bind additional chlorophylls to increase efficiency. The overall reaction
494:
carried out a series of experiments relating to the gases involved in respiration and combustion. In his first experiment, he lit a candle and placed it under an upturned jar. After a short period of time, the candle burned out. He carried out a similar experiment with a
944:
Deisenhofer J, Epp O, Miki K, Huber R, Michel H (December 1984). "X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from
Rhodopseudomonas viridis".
159:
A reaction center is laid out in such a way that it captures the energy of a photon using pigment molecules and turns it into a usable form. Once the light energy has been absorbed directly by the pigment molecules, or passed to them by
368:
collect and transfer the energy from photon absorption: BChl and Bph. BChl roughly resembles the chlorophyll molecule found in green plants, but, due to minor structural differences, its peak absorption wavelength is shifted into the
372:, with wavelengths as long as 1000 nm. Bph has the same structure as BChl, but the central magnesium ion is replaced by two protons. This alteration causes both an absorbance maximum shift and a lowered redox potential.
584:
represents its reduced form. This process of reducing quinone is comparable to that which takes place in the bacterial reaction center. Photosystem II obtains electrons by oxidizing water in a process called
657:
molecules that are bound at the manganese center directly below the pair and extracts an electron from them. This center, below and to the left of the pair in the diagram, contains four manganese ions, a
392:
side of the membrane. This pair of chlorophyll molecules, often called the "special pair", absorbs photons at 870 nm or 960 nm, depending on the species and, thus, is called P870 (for
270:, and plant/cyanobacterial PS-II, use quinones. Not only do all members inside each class share common ancestry, but the two classes also, by means of common structure, appear related.
723:
is a soluble protein containing a 2Fe-2S cluster coordinated by four cysteine residues. The positive charge on the high-energy P700 is neutralized by the transfer of an electron from
309:
The bacterial photosynthetic reaction center has been an important model to understand the structure and chemistry of the biological process of capturing light energy. In the 1960s,
1309:
642:
molecules. In the bacterial reaction center, the electron is obtained from a reduced compound haem group in a cytochrome subunit or from a water-soluble cytochrome-c protein.
408:
standing for "pigment"). Once P absorbs a photon, it ejects an electron, which is transferred through another molecule of Bchl to the BPh in the L subunit. This initial
601:
of oxygen, O, to trace the path of the oxygen from water to gaseous molecular oxygen. This reaction is catalyzed by a reactive center in
Photosystem II containing four
419:. Several factors of the reaction center structure serve to prevent this. First, the transfer of an electron from BPh to P960 is relatively slow compared to two other
134:
exist across the photosynthetic species. Green plants and algae have two different types of reaction centers that are part of larger supercomplexes known as P700 in
1201:
507:
carried out more than 500 experiments spread out over 4 months in an attempt to understand what was really going on. He wrote up his discoveries in a book entitled
1047:
893:
Orf GS, Gisriel C, Redding KE (October 2018). "Evolution of photosynthetic reaction centers: insights from the structure of the heliobacterial reaction center".
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The reaction begins with the excitation of a pair of chlorophyll molecules similar to those in the bacterial reaction center. Due to the presence of chlorophyll
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550:
333:
313:
was the first to purify the reaction center complex from purple bacteria. However, the first crystal structure (upper image at right) was determined in 1984 by
249:
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522:
and his student, William Arnold, used a repetitive flash technique to precisely measure small quantities of oxygen evolved by chlorophyll in the algae
423:
in the reaction center. The faster reactions involve the transfer of an electron from BPh (BPh is oxidized to BPh) to the electron acceptor quinone (Q
671:
electrons. The water molecules that are oxidized in the manganese center are the source of the electrons that reduce the two molecules of Q to QH
638:
The difference between
Photosystem II and the bacterial reaction center is the source of the electron that neutralizes the pair of chlorophyll
161:
47:
1104:
1030:
627:, Photosystem II absorbs light at a shorter wavelength. The pair of chlorophyll molecules at the reaction center are often referred to as
482:
found in green plants, have both photosystems with both types of reaction centers. Combining the two systems allows for producing oxygen.
277:
found in green plants, have both photosystems with both types of reaction centers. Combining the two systems allows for producing oxygen.
593:
with oxygen. The fact that the oxygen from green plants originated from water was first deduced by the
Canadian-born American biochemist
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protein and electron carrier. The plastocyanin complex carries the electron that will neutralize the pair in the next reaction center,
1287:
427:), and the transfer of an electron to P960 (P960 is reduced to P960) from a heme in the cytochrome subunit above the reaction center.
415:
The charges on the P and the BPh could undergo charge recombination in this state, which would waste the energy and convert it into
42:
is a complex of several proteins, pigments, and other co-factors that together execute the primary energy conversion reactions of
773:
438:. This molecule is loosely associated with the protein and is fairly easy to detach. Two electrons are required to fully reduce Q
180:
O to extract electrons and protons from it. In green plants, the electron transport chain has many electron acceptors including
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reactions along the path of a series of protein-bound co-factors. These co-factors are light-absorbing molecules (also named
1000:
412:
yields a positive charge on P and a negative charge on the BPh. This process takes place in 10 picoseconds (10 seconds).
1275:
1051:
849:"Conservation of distantly related membrane proteins: photosynthetic reaction centers share a common structural core"
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Every time the P680 absorbs a photon, it gives off an electron to pheophytin, gaining a positive charge. After this
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bacteria is currently best understood, since it was the first reaction center of known structure and has fewer
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in 1988. This was also significant for being the first 3D crystal structure of any membrane protein complex.
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Four different subunits were found to be important for the function of the photosynthetic reaction center.
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directly above that, through three 4Fe-4S clusters, and finally to an interchangeable ferredoxin complex.
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is used to pump protons across the membrane to the periplasmic space. The electrons from the cytochrome bc
229:
193:
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310:
980:
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349:
345:
262:, and plant/cyanobacterial PS-I, use iron sulfur clusters as electron acceptors. Type II, found in
63:
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of the plasma membrane. They are structurally similar to one another, both having 5 transmembrane
208:. The passage of the electron through the electron transport chain also results in the pumping of
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225:
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466:-complex are then transferred through a soluble cytochrome c intermediate, called cytochrome c
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55:
17:
589:. Molecular oxygen is a byproduct of this process, and it is this reaction that supplies the
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The cooperation between
Photosystems I and II creates an electron and proton flow from H
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steps ultimately result in the conversion of the energy of photons to chemical energy.
43:
958:
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1257:
1240:
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1096:
1087:
Jagannathan B, Golbeck J (2009). "Photosynthesis: microbial". In
Schaechter M (ed.).
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O to NADP, producing NADPH needed for glucose synthesis. This pathway is called the '
700:
341:
337:
259:
189:
135:
46:. Molecular excitations, either originating directly from sunlight or transferred as
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237:
233:
34:
Electron micrograph of a 2D crystal of the LH1-Reaction center photosynthetic unit.
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bacterial reaction center, and it is theorized that they share a common ancestor.
388:
The process starts when light is absorbed by two BChl molecules that lie near the
1179:
446:, taking up two protons from the cytoplasm in the process. The reduced quinone QH
1235:
997:
789:
710:
molecules initiates photoinduced charge separation. This pair is referred to as
706:
As with
Photosystem II and the bacterial reaction center, a pair of chlorophyll
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The high-energy electron that resides on the tightly bound quinone molecule Q
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336:, shown in blue and purple in the image of the structure, both span the
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353:
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185:
142:. The structures of these supercomplexes are large, involving multiple
103:
914:
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Schematic of reaction center in the membrane, with
Cytochrome C at top
1319:
1314:
1210:
696:
285:
This section deals with the type II system found in purple bacteria.
205:
79:
1048:"Oxygenic photosynthesis: Bacterial growth and microbial metabolism"
1023:
Probing photosynthesis : mechanisms, regulation, and adaptation
731:
back to Q. Thus the overall reaction catalyzed by
Photosystem I is:
458:) where it is oxidized. In the process the reducing power of the QH
94:, for a transfer of hydrogen atoms (as protons and electrons) from H
679:
catalytic center has not been reproduced by any man-made catalyst.
1404:
1399:
757:
687:
After the electron has left Photosystem II it is transferred to a
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379:
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29:
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Two classes of reaction centres are recognized. Type I, found in
204:, while the energy used to split water results in the release of
1297:
1292:
711:
628:
605:
416:
27:
Molecular unit responsible for absorbing light in photosynthesis
1183:
500:
demonstrated the activity of a photosynthetic reaction center.
1151:(2–3). University of Illinois at Urbana-Champaign: 179–214.
450:
diffuses through the membrane to another protein complex (
580:
Q represents the oxidized form of plastoquinone while QH
727:, which receives energy eventually used to convert QH
1310:
Branched-chain alpha-keto acid dehydrogenase complex
764:
O to NADP via P680 and P700 resembles the letter Z.
434:
is transferred to an exchangeable quinone molecule Q
1412:
Phosphoenolpyruvate sugar phosphotransferase system
1340:
1256:
1221:
826:"Chapter 19: The Light Reactions of Photosynthesis"
998:Photosynthetic reaction centers of purple bacteria
236:molecule. Both the ATP and NADPH are used in the
538:Cyanobacteria photosystem II, Monomer, PDB 2AXT.
114:Transforming light energy into charge separation
1231:Photosynthetic reaction center complex proteins
819:
817:
815:
200:, which result finally in the reduced molecule
888:
886:
884:
470:, in the periplasm to the cytochrome subunit.
1195:
1124:. University of Illinois at Urbana-Champaign.
800:Photosynthetic reaction center protein family
250:Photosynthetic reaction center protein family
176:and pass energy to a hydrogen donor such as H
102:towards carbon dioxide, eventually producing
8:
224:, resulting in a proton gradient across the
90:created is then used, via a chain of nearby
1202:
1188:
1180:
1021:. In Yunus M, Pathre U, Mohanty P (eds.).
1007:(2 February 1999). Retrieved Feb 28, 2010.
240:to fix carbon dioxide into triose sugars.
118:Reaction centers are present in all green
1019:"Chapter 1: Milestones in Photosynthesis"
864:
305:Bacterial photosynthetic reaction center.
1122:"The Z-Scheme Diagram of Photosynthesis"
653:of high energy. It passes its energy to
824:Berg JM, Tymoczko JL, Stryer L (2002).
811:
549:The core of Photosystem II consists of
635:as well as the uptake of two protons.
832:(5th ed.). New York: WH Freeman.
551:two subunits referred to as D1 and D2
7:
1395:Mitochondrial trifunctional protein
981:"The Nobel Prize in Chemistry 1988"
156:than the examples in green plants.
1091:(3rd ed.). pp. 325–341.
714:, where 700 is a reference to the
25:
1097:10.1016/B978-012373944-5.00352-7
1025:. London: Taylor & Francis.
776:(oxygen in biological processes)
774:Dioxygen in biological reactions
478:Cyanobacteria, the precursor to
273:Cyanobacteria, the precursor to
52:light-harvesting antenna systems
1353:Carbamoyl phosphate synthase II
853:Molecular Biology and Evolution
352:molecules (BPh) molecules, two
228:that can be used to synthesize
146:. The reaction center found in
1358:Aspartate carbamoyltransferase
1266:Pyruvate dehydrogenase complex
1141:"Photosynthesis Web Resources"
1046:Kaiser GE (24 February 2003).
647:photoinduced charge separation
40:photosynthetic reaction center
18:Photosynthetic reaction center
1:
1390:Glycine decarboxylase complex
1385:Fatty acid synthetase complex
959:10.1016/S0022-2836(84)80011-X
1089:Encyclopedia of Microbiology
947:Journal of Molecular Biology
281:In purple bacteria (type II)
1139:Orr L, Govindjee R (2013).
509:Experiments upon Vegetables
474:In Cyanobacteria and plants
1474:
1458:Integral membrane proteins
1422:Sucrase-isomaltase complex
1288:Oxoglutarate dehydrogenase
615:Electron transport in PS2.
325:for which they shared the
247:
144:light-harvesting complexes
132:light-harvesting complexes
1157:10.1007/s11120-013-9840-3
907:10.1007/s11120-018-0503-2
212:(hydrogen ions) from the
1380:Electron transport chain
843:Sadekar, S; Raymond, J;
780:Light-harvesting complex
649:, P680 is a very strong
348:(BChl-b) molecules, two
174:electron transport chain
166:light-harvesting complex
1370:P450-containing systems
1145:Photosynthesis Research
895:Photosynthesis Research
486:Oxygenic photosynthesis
395:Rhodobacter sphaeroides
1375:Cytochrome b6f complex
689:cytochrome b6f complex
616:
557:by Photosystem II is:
539:
385:
306:
298:
35:
1215:multienzyme complexes
866:10.1093/molbev/msl079
614:
537:
490:In 1772, the chemist
401:Blastochloris viridis
383:
346:bacteriochlorophyll b
304:
296:
256:green-sulfur bacteria
248:Further information:
82:is used to excite an
33:
1017:Govindjee R (2000).
350:bacteriopheophytin b
334:The L and M subunits
78:. The energy of the
1427:Tryptophan synthase
1417:Polyketide synthase
625:bacteriochlorophyll
164:from a surrounding
1003:2006-05-14 at the
617:
595:Martin David Kamen
540:
386:
384:The light reaction
319:Johann Deisenhofer
307:
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226:thylakoid membrane
162:resonance transfer
154:polypeptide chains
92:electron acceptors
86:of a pigment. The
36:
1435:
1434:
1106:978-0-12-373944-5
1076:on 3 August 2003.
1066:"The chloroplast"
1032:978-0-7484-0821-4
847:(November 2006).
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410:charge separation
108:electron transfer
56:electron transfer
48:excitation energy
16:(Redirected from
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675:. To date, this
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492:Joseph Priestley
311:Roderick Clayton
149:Rhodopseudomonas
100:hydrogen sulfide
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953:(2): 385–98.
952:
948:
940:
937:
932:
928:
924:
920:
916:
912:
908:
904:
900:
896:
889:
887:
885:
881:
876:
872:
867:
862:
858:
854:
850:
846:
839:
836:
831:
827:
820:
818:
816:
812:
805:
801:
798:
796:
795:Phycobilisome
793:
791:
788:
786:
783:
781:
778:
775:
772:
771:
767:
765:
759:
755:
742:→ Pc(Cu) + Fd
741:
734:
733:
732:
726:
722:
717:
713:
709:
704:
702:
701:Photosystem I
698:
694:
690:
683:Photosystem I
682:
680:
678:
669:
665:
661:
656:
652:
648:
643:
641:
636:
630:
626:
622:
613:
609:
607:
604:
600:
596:
592:
588:
568:
560:
559:
558:
556:
552:
547:
544:
536:
529:
527:
525:
521:
516:
514:
510:
506:
501:
498:
493:
485:
483:
481:
473:
471:
457:
452:cytochrome bc
428:
422:
418:
413:
411:
407:
403:
402:
397:
396:
391:
382:
375:
373:
371:
365:
355:
351:
347:
343:
342:alpha helices
339:
338:lipid bilayer
335:
330:
328:
324:
320:
316:
312:
303:
295:
288:
286:
280:
278:
276:
271:
269:
265:
261:
260:Heliobacteria
257:
251:
243:
241:
239:
235:
231:
227:
223:
220:and into the
219:
215:
211:
207:
203:
199:
195:
194:cytochrome bf
191:
190:plastoquinone
187:
183:
175:
171:
167:
163:
157:
155:
151:
150:
145:
141:
137:
136:Photosystem I
133:
129:
125:
121:
113:
111:
109:
105:
101:
93:
89:
85:
81:
77:
74:, as well as
73:
69:
65:
61:
57:
53:
49:
45:
41:
32:
19:
1230:
1148:
1144:
1115:
1088:
1082:
1074:the original
1069:
1060:
1052:the original
1041:
1022:
1012:
993:
984:
975:
950:
946:
939:
901:(1): 11–37.
898:
894:
856:
852:
838:
830:Biochemistry
829:
747:
739:
725:plastocyanin
707:
705:
693:plastocyanin
691:and then to
686:
644:
639:
637:
620:
618:
597:. He used a
579:
566:
548:
541:
523:
517:
508:
502:
489:
480:chloroplasts
477:
429:
414:
405:
399:
393:
387:
366:
331:
323:Robert Huber
308:
284:
275:chloroplasts
272:
264:chloroflexus
253:
238:Calvin cycle
234:ATP synthase
158:
147:
138:and P680 in
117:
60:chromophores
39:
37:
1236:Photosystem
790:Photosystem
735:Pc(Cu) + Fd
666:ion, and a
390:periplasmic
327:Nobel Prize
214:chloroplast
126:, and many
88:free energy
68:chlorophyll
1442:Categories
806:References
721:Ferredoxin
716:wavelength
591:atmosphere
587:photolysis
232:using the
198:ferredoxin
182:pheophytin
72:pheophytin
66:) such as
1173:254943144
695:, a blue
603:manganese
555:catalyzed
524:Chlorella
518:In 1932,
503:In 1779,
376:Mechanism
289:Structure
170:electrons
1165:23708976
1001:Archived
923:29603081
875:16887904
768:See also
754:Z-scheme
668:tyrosine
664:chloride
456:-complex
404:), with
370:infrared
354:quinones
172:into an
128:bacteria
106:. These
84:electron
76:quinones
64:pigments
1211:Enzymes
967:6392571
931:4473759
915:1494566
662:ion, a
660:calcium
651:oxidant
561:2Q + 2H
344:. Four
210:protons
186:quinone
104:glucose
1320:BCKDHB
1315:BCKDHA
1171:
1163:
1103:
1029:
965:
929:
921:
913:
873:
697:copper
515:air'.
218:stroma
206:oxygen
196:, and
120:plants
80:photon
1405:HADHB
1400:HADHA
1341:Other
1169:S2CID
927:S2CID
758:redox
655:water
573:+ 2QH
497:mouse
442:to QH
360:and Q
222:lumen
202:NADPH
124:algae
98:O or
1298:DLST
1293:OGDH
1161:PMID
1101:ISBN
1027:ISBN
963:PMID
919:PMID
911:OSTI
871:PMID
712:P700
629:P680
606:ions
565:O +
417:heat
321:and
70:and
50:via
1348:CAD
1330:DLD
1325:DBT
1303:DLD
1153:doi
1149:115
1093:doi
955:doi
951:180
903:doi
899:138
861:doi
569:→ O
230:ATP
216:'s
62:or
1444::
1281:E3
1276:E2
1271:E1
1246:II
1213::
1167:.
1159:.
1147:.
1143:.
1099:.
1068:.
983:.
961:.
949:.
925:.
917:.
909:.
897:.
883:^
869:.
857:23
855:.
851:.
828:.
814:^
740:hν
738:+
703:.
608:.
567:hν
356:(Q
317:,
266:,
258:,
192:,
188:,
184:,
122:,
38:A
1241:I
1203:e
1196:t
1189:v
1175:.
1155::
1109:.
1095::
1035:.
987:.
969:.
957::
933:.
905::
877:.
863::
762:2
750:2
729:2
708:a
673:2
640:a
633:2
621:a
582:2
575:2
571:2
563:2
468:2
464:1
460:2
454:1
448:2
444:2
440:B
436:B
432:A
425:A
406:P
362:B
358:A
178:2
96:2
20:)
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