Summary
Photosynthetic non-oxygenic purple bacteria possess various energy-conserving machineries that allow them to grow either photosynthetically, anaerobically or aerobically. The photosynthetic and respiratory branches of the power system in purple bacteria are connected via the cytochrome bc 1 complex (cyt bc 1), which catalyzes electron transfer from quinol to cyt c and couples this reaction to proton translocation across the photosynthetic membrane, generating a trans-membrane proton gradient essential for various cellular activities including ATP synthesis. Crystal structures of wild-type and mutant cyt bc 1 complexes have been determined for the closely related photosynthetic bacteria R. sphaeroides and R. capsulatus in the presence of various inhibitors or substrates. These structures are remarkably similar to their mitochondrial counterparts but do feature insertions or deletions that are characteristic of the bacterial enzyme complexes. Thus, it is expected that bacterial cyt bc 1 complexes function in a manner similar to mitochondrial enzymes, justifying their use as model systems. The roles of insertions in bacterial cyt bc 1 function are discussed in relation to the subunit compositions of bacterial complexes and to mutagenesis studies. The mechanism of cyt bc 1 function is also discussed in the context of the architecture of quinol oxidation and quinone reduction sites, as revealed by inhibitor binding studies of both mitochondrial and bacterial bc 1 complexes.
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- Btbc 1 :
-
Bos taurus mitochondrial bc 1
- cyt bc 1 :
-
Ubiquinol-cytochrome c oxidoreductase cytochrome bc 1 or bc 1
- cyt:
-
Cytochrome
- famoxadone:
-
(S)-5-Methyl-5-(4-phenoxy-phenyl)-3-(phenylamino)-1,3-oxazolidine-2,4-dione
- fenamidone:
-
(RS)-5-Methyl-2- (methylsulfanyl)-5-phenyl-3-(phenylamino)-3,5-dihydro-4H-imidazol-4-one
- Ggbc 1 :
-
Gallus gallus mitochondrial bc 1
- IMS:
-
Inter-membrane space
- ISP:
-
Iron-sulfur protein
- ISP-ED:
-
Extrinsic domain of ISP
- JG144:
-
3-anilino-5-(2,4-difluoro-phenyl)-5-methyl-oxazol-idine-2,4-dione
- LHC:
-
Light-harvesting complex
- Mtbc 1 :
-
Mitochondrial bc 1
- NCS:
-
Non-crystallographic symmetry
- Pdbc 1 :
-
bc 1 from Paracoccus denitrificans
- pmf:
-
Proton motive force
- Q:
-
Ubiquinone
- QH2 :
-
Ubiquinol
- QN :
-
Ubiquinone reduction
- QP :
-
Ubiquinol oxidation
- RC:
-
Bacterial reaction center
- Rcbc 1 :
-
bc 1 from Rhodobacter capsulatus
- rms deviation:
-
Root-mean square deviation
- Rsbc 1 :
-
bc 1 from the photosynthetic bacterium Rhodobacter sphaeroides
- SAMICS:
-
Surface affinity-modulated ISP-ED conformation switch mechanism
- Scbc 1 :
-
Saccharomyces cerevisiae mitochondrial bc 1
- TM:
-
Trans-membrane
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Acknowledgments
The authors wish to thank George Leiman for editorial assistance. This research was supported by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research.
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Esser, L., Zhou, F., Yu, CA., Xia, D. (2016). Structure-Function Studies of the Cytochrome bc 1 Complex of Anoxygenic Photosynthetic Purple Bacteria. In: Cramer, W., Kallas, T. (eds) Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling. Advances in Photosynthesis and Respiration, vol 41. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-7481-9_10
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