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Electron Transfer Reactions at the Qo Site of the Cytochrome bc 1 Complex: The Good, the Bad, and the Ugly

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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

The cytochrome bc 1 complex of eukaryotic mitochondrial and prokaryotic energy transducing membranes functions as a protonmotive quinol:cytochrome c oxidoreductase. The enzyme utilizes a highly characteristic ‘Q-cycle’ reaction mechanism in which oxidation of substrate quinol leads to a bifurcated electron transfer pathway. This mechanism generates a highly-reducing, reactive radical semiquinone (SQo) intermediate at the site of quinol oxidation (Qo) within cytochrome b which must be tightly managed to prevent energetically wasteful electron transfer side reactions or reduction of dioxygen to biologically harmful superoxide. In this chapter we discuss mechanistic strategies harnessed by the bc 1 complex to minimize unproductive electron transfer from SQo with particular reference to superoxide generation. Recent work suggests that the bc 1 complex achieves this by kinetically trapping the SQo anion within a hydrophobic region of the Qo pocket as a destabilized, low-occupancy intermediate, conserving redox energy to reduce the native electron acceptor (ferriheme b L) while minimizing the probability of unwanted (and potentially damaging) electron transfer bypass reactions.

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Abbreviations

[2Fe-2S]:

The iron-sulfur cluster of the ‘Rieske’ iron-sulfur protein

Cyt:

Cytochrome

ENDOR:

Electron nuclear double resonance spectroscopy

EPR:

Electron paramagnetic resonance spectroscopy

ESEEM:

Electron spin echo envelope modulation spectroscopy

HHDBT:

5-n-heptyl- 6-hydroxy-4,7-dioxobenzothiazole

ISP:

The ‘Rieske’ iron-sulfur protein

PEWY:

The Pro271-Glu-Trp-Tyr274 sequence within the Qo site of cytochrome b (yeast numbering)

QH2 :

Quinol or hydroquinone

Qi :

Quinone reductase site of the cytochrome bc 1 complex

Qo :

Quinol oxidase site of the cytochrome bc 1 complex

SQ:

Semiquinone

SQo :

Semiquinone associated with the quinol oxidase site of the cytochrome bc 1 complex

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Acknowledgments

Financial support from the National Institute of General Medical Sciences of the National Institutes of Health (R01GM061904 to MKB) and the Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the US Department of Energy (DE-FG02-11ER16220 to DMK) is gratefully acknowledged. Foundational support for the Plant Research Lab provided by Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the US Department of Energy Grant DE-FG02-91ER20021.

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Authors and Affiliations

  1. MSU-DOE Plant Research Laboratory, and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA

    Nicholas Fisher & David M. Kramer

  2. Department of Chemistry, The University of Alabama, Tuscaloosa, AL, 35487-0336, USA

    Michael K. Bowman

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  1. Nicholas Fisher
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  2. Michael K. Bowman
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Correspondence to David M. Kramer .

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Editors and Affiliations

  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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Fisher, N., Bowman, M.K., Kramer, D.M. (2016). Electron Transfer Reactions at the Qo Site of the Cytochrome bc 1 Complex: The Good, the Bad, and the Ugly. 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_21

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