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The Cytochrome bc 1 and Related bc Complexes: The Rieske/Cytochrome b Complex as the Functional Core of a Central Electron/Proton Transfer Complex

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The Purple Phototrophic Bacteria

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 28))

Summary

The cytochrome (Cyt) bc 1 and related complexes play a central role in purple bacterial photosynthesis, transferring electrons between electron carriers reduced and oxidized by the photochemical reaction centers, oxidizing quinol (QH2) and reducing Cyt c while translocating protons via some variation of the Q-cycle mechanism. In this chapter, we discuss recent advances in the biochemical, biophysical and evolutionary understanding of these complexes. The mechanistic core of these complexes, conserved over billions of years, contains the Cyt b protein (with its two associated b-type hemes) and the Rieske iron-sulfur center. Together, this central core performs the central (and well-conserved) reaction of the Q-cycle, that is the ‘bifurcated’ oxidation of QH2 at the quinol oxidation (Qo) site, with two electrons sent to different acceptors, one to the Rieske iron-sulfur center and the other to the Cyt b chain. The subsequent reactions of the Q-cycle, involving the reduction of secondary carriers (a high potential Cyt c in the case of purple bacteria) and quinone at the quinone reduction (Qi) site are less well conserved both in terms of structure and mechanism. We thus use the term Rieske/Cytochrome b (RB) complexes for these enzymes. Key issues surrounding the mechanisms of the RB complexes are discussed, including a series of currently debated models for the avoidance of deleterious side reactions within the Qo site, the mechanism of stabilization of semiquinone intermediates within the Qi site, and the role of the pivoting iron-sulfur protein subunit.

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Abbreviations

[2Fe-2S]:

the ‘Rieske’ iron-sulfur center of the iron sulfur protein

AA:

antimycin A

C:

high potential electron carriers that accept electrons from the [2Fe-2S] center

CW-EPR:

continuous wave-electron paramagnetic resonance

Cyt:

cytochrome

Em :

redox midpoint potential

EPR:

electron paramagnetic resonance

HQNO:

2-n-heptyl-4-hydroxyquinoline-N-oxide

ISP:

iron-sulfur protein subunit

k SOP :

the rate constant for reduction of O2 by SQ

KSQ :

the equilibrium constant for oxidation of QH2 to SQ

LUCA:

last universal common ancestor

MOA-stilbene:

E-β-methoxyacrylate-stilbene

pmf :

proton motive force

Q:

quinone

QB :

the quinone reductase site of type II reaction centers

QH2 :

quinol or hydroquinone

Qi :

quinone reductase site of the RB complexes

Qo :

quinol oxidase site of the RB complexes

RB:

Rieske/Cytochrome b

SC:

secondary electron carriers

SQ:

semiquinone (the term ‘SQ’is used to indicate both the anion (Q·−) and neutral (Q·H) forms)

UQ:

ubiquinone

UQH2 :

ubiquinol

vSOP :

velocity of Superoxide production

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Authors and Affiliations

  1. Institute of Biological Chemistry, Washington State University, Pullman, WA, 99164-6340, USA

    David M. Kramer

  2. Laboratoire de Bioénergétique et Ingénierie des Protéines, Institut de Biologie Structurale et Microbiologie, CNRS, 13402, Marseille, France

    Wolfgang Nitschke

  3. Department of Chemistry, University of Missouri-Columbia, Columbia, MO, 65211, USA

    Jason W. Cooley

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  1. David M. Kramer
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  2. Wolfgang Nitschke
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  3. Jason W. Cooley
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Correspondence to David M. Kramer .

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Editors and Affiliations

  1. University of Sheffield, UK

    C. Neil Hunter

  2. University of Pennsylvania, USA

    Fevzi Daldal

  3. Argonne National Laboratory, USA

    Marion C. Thurnauer

  4. University of British Columbia, Canada

    J. Thomas Beatty

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Kramer, D.M., Nitschke, W., Cooley, J.W. (2009). The Cytochrome bc 1 and Related bc Complexes: The Rieske/Cytochrome b Complex as the Functional Core of a Central Electron/Proton Transfer Complex. In: Hunter, C.N., Daldal, F., Thurnauer, M.C., Beatty, J.T. (eds) The Purple Phototrophic Bacteria. Advances in Photosynthesis and Respiration, vol 28. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-8815-5_23

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