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Structure-Function Studies of the Cytochrome bc 1 Complex of Anoxygenic Photosynthetic Purple Bacteria

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Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 41))

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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Abbreviations

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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Authors and Affiliations

  1. Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, 20892, USA

    Lothar Esser, Fei Zhou & Di Xia

  2. Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK, 74078, USA

    Chang-An Yu

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  1. Lothar Esser
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  2. Fei Zhou
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  3. Chang-An Yu
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  4. Di Xia
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Correspondence to Di Xia .

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  1. Department of Biological Sciences, Purdue University, West Lafayette, Indiana, USA

    William A. Cramer

  2. Department of Biology, University of Wisconsin-Oshkosh, Oshkosh, Wisconsin, USA

    Toivo Kallas

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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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