Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.

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...

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Main Authors:	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.
Format:	Online
Language:	English
Published:	Nature Publishing Group 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4486940/

id	pubmed-4486940
recordtype	oai_dc
spelling	pubmed-44869402015-07-08 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. Article 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. Nature Publishing Group 2015-07-01 /pmc/articles/PMC4486940/ /pubmed/26126857 http://dx.doi.org/10.1038/srep11677 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	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.
spellingShingle	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. Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.
author_facet	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.
author_sort	Edwards, Marcus J.
title	Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.
title_short	Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.
title_full	Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.
title_fullStr	Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.
title_full_unstemmed	Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.
title_sort	redox linked flavin sites in extracellular decaheme proteins involved in microbe-mineral electron transfer.
description	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.
publisher	Nature Publishing Group
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4486940/
_version_	1613242124550012928

Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.

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