REVIEW: Structural and Functional Studies of Multiheme Cytochromes c Involved in Extracellular Electron Transport in Bacterial Dissimilatory Metal Reduction

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T. V. Tikhonova^* and V. O. Popov

Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia; E-mail: ttikhonova@inbi.ras.ru

^* To whom correspondence should be addressed.

Received July 18, 2014

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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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KEY WORDS: bacterial dissimilatory metal reduction, extracellular electron transfer, multiheme cytochrome c

DOI: 10.1134/S0006297914130094

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