Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 23, Pages 9384-9389Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1017200108
Keywords
c-type cytochromes; iron respiration; MtrC; multiheme
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Funding
- US Department of Energy, Office of Biological and Environmental Research
- Royal Society Wolfson Foundation
- Biotechnology and Biological Sciences Research Council [H007288/1]
- BBSRC [BB/H007288/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H007288/1] Funding Source: researchfish
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Some bacterial species are able to utilize extracellular mineral forms of iron and manganese as respiratory electron acceptors. In Shewanella oneidensis this involves decaheme cytochromes that are located on the bacterial cell surface at the termini of transouter-membrane electron transfer conduits. The cell surface cytochromes can potentially play multiple roles in mediating electron transfer directly to insoluble electron sinks, catalyzing electron exchange with flavin electron shuttles or participating in extracellular intercytochrome electron exchange along nanowire appendages. We present a 3.2-angstrom crystal structure of one of these decaheme cytochromes, MtrF, that allows the spatial organization of the 10 hemes to be visualized for the first time. The hemes are organized across four domains in a unique crossed conformation, in which a staggered 65-angstrom octaheme chain transects the length of the protein and is bisected by a planar 45-angstrom tetraheme chain that connects two extended Greek key split beta-barrel domains. The structure provides molecular insight into how reduction of insoluble substrate (e. g., minerals), soluble substrates (e. g., flavins), and cytochrome redox partners might be possible in tandem at different termini of a trifurcated electron transport chain on the cell surface.
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