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DOI:10.1021/BI049444O - Corpus ID: 17097971
@article{Cramer2004EvolutionOP, title={Evolution of photosynthesis: time-independent structure of the cytochrome b6f complex.}, author={William A. Cramer and Huamin Zhang and Jiusheng Yan and Genji Kurisu and Janet L. Smith}, journal={Biochemistry}, year={2004}, volume={43 20}, pages={ 5921-9 }, url={https://api.semanticscholar.org/CorpusID:17097971}}
- W. Cramer, Huamin Zhang, Janet L. Smith
- Published in Biochemistry 25 May 2004
- Biology, Chemistry, Environmental Science
The structure and position of heme x suggest that it could function in ferredoxin-dependent cyclic electron transport as well as being an intermediate in a quinone cycle mechanism for electron and proton transfer.
56 Citations
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56 Citations
- W. CramerHuamin ZhangJiusheng YanG. KurisuJanet L. Smith
- 2006
Biology, Chemistry
Annual review of biochemistry
Crystal structures and their implications for function are described for the energy transducing hetero-oligomeric dimeric cytochrome b6f complex of oxygenic photosynthesis from the thermophilic…
- 160
- E. BerryLi-shar HuangL. K. SaechaoN. PonM. Valkova-ValchanovaF. Daldal
- 2004
Biology, Chemistry
Photosynthesis Research
A preliminary X-ray structure of Rhodobacter capsulatus cyt bc1 is presented and compared to the available structures of its hom*ologues from mitochondria and chloroplast and the structural similarities and differences that are found among the three catalytic subunits between the members of this family of enzymes are highlighted.
- 176
- PDF
- W. CramerE. Yamash*taD. BaniulisS. Hasan
- 2010
Biology, Environmental Science
The cytochrome b6f complex is the central complex in the electron transport chain of oxygenic photosynthesis. It provides the electronic connection between the two photosynthetic reaction centers and…
- 7
- E. BerryDong Woo LeeLi-shar HuangF. Daldal
- 2009
Biology, Chemistry
Recent progress illustrates that the cytochrome bc 1 provides an invaluable model system for studying the mechanism of redox driven proton translocation across energy transducing membranes.
- 12
- G. BernátM. Rögner
- 2011
Biology, Environmental Science
The cytochrome b 6 f complex is a shared, central component of both photosynthetic and respiratory electron- and proton transport in cyanobacteria and its function within the cyanobacterial electron transport network is reviewed.
- 15
- W. CramerJiusheng YanHuamin ZhangG. KurisuJanet L. Smith
- 2004
Biology, Chemistry
Photosynthesis Research
Three-Å crystal structures of the cytochrome b6f complex have provided a structural framework for the photosynthetic electron transport chain and several functional insights have emerged including the function of the dimer; the properties of heme x.
- 38
- J. AlricY. PierreD. PicotJ. LavergneF. Rappaport
- 2005
Chemistry, Biology
Proceedings of the National Academy of Sciences…
The spectrum of c(i) matches the absorption changes previously observed in vivo for an unknown redox center denoted "G," and the effect of the membrane potential on the electron transfer equilibrium between G and heme b(H) found in earlier experiments is discussed.
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- PDF
- Bin-Xing LiD. MaoYulong LiuLiangbi LiT. Kuang
- 2004
Biology, Environmental Science
Photosynthesis Research
A pure, active cytochrome b6f was isolated from the chloroplasts of the marine green alga, Bryopsiscorticulans. To investigate and characterize this cytochrome b6f complex, sodium dodecyl…
- 11
- W. CramerS. HasanE. Yamash*ta
- 2011
Chemistry, Biology
Biochimica et biophysica acta
- 152
- PDF
- D. DibrovaD. ShalaevaMichael Y. GalperinA. Mulkidjanian
- 2017
Biology, Environmental Science
Physiologia plantarum
This analysis provides further support to the earlier suggestion that the ancestral version of cyt bc complex contained a small four‐helical cyt b with three hemes similar to the plant cytochrome b 6 and independent fusion events led to the formation of large cyts b in several lineages.
- 15
- PDF
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104 References
- G. KurisuHuamin ZhangJanet L. SmithW. Cramer
- 2003
Chemistry, Biology
Science
The dimeric b6f complex from the thermophilic cyanobacterium Mastigocladus laminosus reveals a large quinone exchange cavity, stabilized by lipid, in which plastoquinone, a quin one-analog inhibitor, and a novel heme are bound.
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- David StroebelY. ChoquetJ. PopotD. Picot
- 2003
Chemistry, Biology
Nature
The X-ray structure of cytochrome b6f from the alga Chlamydomonas reinhardtii is presented and it is shown that this haem is atypical as it is covalently bound by one thioether linkage and has no axial amino acid ligand, which may be the missing link in oxygenic photosynthesis.
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- PDF
- W. CramerG. M. Soriano Janet L. Smith
- 1996
Biology, Environmental Science
Annual review of plant physiology and plant…
An unusual electron transfer event, the oxidant-induced reduction of a significant fraction of the p (lumen)-side cytochrome b heme by plastosemiquinone indicates that the electron transfer pathway in the b6f complex can be described by a version of the Q-cycle mechanism.
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- P. N. FurbacherM. GirvinW. Cramer
- 1989
Biology, Chemistry
Biochemistry
Examination of the redox properties, the site of action of the inhibitor NQNO, and the question of interheme transfer in the chloroplast cytochrome b6 have been examined, providing no evidence for efficient electron transfer from heme bp to heme ba as specified by the Q cycle model.
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Biology, Environmental Science
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- P. JoliotA. Joliot
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Biology, Chemistry
Proceedings of the National Academy of Sciences…
Flash-induced kinetics of the redox changes of Cyt b and of the formation of a transmembrane potential have been measured in Chlorella sorokiniana cells incubated in reducing conditions that induce a full reduction of the plastoquinone pool.
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- Zhaolei ZhangLisha Huang Sung-Hou Kim
- 1998
Chemistry, Biology
Nature
X-ray crystal structures of the cytochrome bc1 complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein.
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- E. DarrouzetM. Valkova-ValchanovaC. MoserP. DuttonF. Daldal
- 2000
Chemistry, Biology
Proceedings of the National Academy of Sciences…
It is demonstrated that this domain movement is essential for cyt bc(1) function, because a mutant enzyme with a nonmoving Fe-S subunit has no catalytic activity, and one with a slower movement has lower activity.
- 127
- PDF
- C. J. CarrellHuamin ZhangW. CramerJanet L. Smith
- 1997
Biology
Structure
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- H. ZhangJ. WhiteleggeW. Cramer
- 2001
Biology, Chemistry
The Journal of biological chemistry
Electrospray ionization mass spectrometry of CNBr fragments of the 35-kDa polypeptide was diagnostic for ferredoxin:NADP+ oxidoreductase (FNR), as were antibody reactivity to FNR and diaphorase activity.
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- PDF
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