Redox linked flavin sites in extracellular decaheme proteins involved in microbe-mineral electron transfer.

Edwards, Marcus J.; White, Gaye F.; Norman, Michael; Tome-Fernandez, Alice; Ainsworth, Emma; Shi, Liang; Fredrickson, Jim K.; Zachara, John M.; Butt, Julea N.; Richardson, David J.; Clarke, Thomas A.

doi:10.1038/srep11677

Title: Redox linked flavin sites in extracellular decaheme proteins involved in microbe-mineral electron transfer.

Journal Article · Wed Jul 01 00:00:00 EDT 2015 · Scientific Reports

DOI:https://doi.org/10.1038/srep11677· OSTI ID:1203147

Edwards, Marcus J. ^[1]; White, Gaye F. ^[1]; Norman, Michael ^[1]; Tome-Fernandez, Alice ^[1]; Ainsworth, Emma ^[1]; Shi, Liang ^[2]; Fredrickson, Jim K. ^[2]; Zachara, John M. ^[2]; Butt, Julea N. ^[1]; Richardson, David J. ^[1]; Clarke, Thomas A. ^[1]

Univ. of East Anglia, Norwich (United Kingdom)
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)

Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism of electron exchange at the interface between cytochrome and acceptor is widely debated. The 1.8 Å x-ray crystal structure of the decaheme MtrC revealed a highly conserved CX₈C disulfide that, when substituted for AX₈A, severely compromised the ability of S. oneidensis to grow under aerobic conditions. Reductive cleavage of the disulfide in the presence of flavin mononucleotide (FMN) resulted in the reversible formation of a stable flavocytochrome. Similar results were also observed with other decaheme cytochromes, OmcA, MtrF and UndA. The data suggest that these decaheme cytochromes can transition between highly reactive flavocytochromes or less reactive cytochromes, and that this transition is controlled by a redox active disulfide that responds to the presence of oxygen.

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Research Organization:: Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC05-76RL01830

OSTI ID:: 1203147

Journal Information:: Scientific Reports, Vol. 5; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 118 works

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