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Structural and functional studies of multiheme cytochromes c involved in extracellular electron transport in bacterial dissimilatory metal reduction

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Abstract

Bacteria utilizing insoluble mineral forms of metal oxides as electron acceptors in respiratory processes are widespread in the nature. The electron transfer from a pool of reduced quinones in the cytoplasmic membrane across the periplasm to the bacterial outer membrane and then to an extracellular acceptor is a key step in bacterial dissimilatory metal reduction. Multiheme cytochromes c play a crucial role in the extracellular electron transfer. The bacterium Shewanella oneidensis MR-1 was used as a model organism to study the mechanism of extracellular electron transport. In this review, we discuss recent data on the composition, structures, and functions of multiheme cytochromes c and their functional complexes responsible for extracellular electron transport in Shewanella oneidensis.

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Abbreviations

BDMR:

bacterial dissimilatory metal reduction

ETC:

electron transport chain

Fe-NTA:

iron nitrilotriacetate

OMC:

outer-membrane cytochrome c

rmsd:

root-meansquare deviation

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  1. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071, Moscow, Russia

    T. V. Tikhonova & V. O. Popov

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Original Russian Text © T. V. Tikhonova, V. O. Popov, 2014, published in Uspekhi Biologicheskoi Khimii, 2014, Vol. 54, pp. 349–384.

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Tikhonova, T.V., Popov, V.O. Structural and functional studies of multiheme cytochromes c involved in extracellular electron transport in bacterial dissimilatory metal reduction. Biochemistry Moscow 79, 1584–1601 (2014). https://doi.org/10.1134/S0006297914130094

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