Antibody Recognition Force Microscopy Shows that Outer Membrane Cytochromes OmcA and MtrC Are Expressed on the Exterior Surface of
            <i>Shewanella oneidensis</i>
            MR-1

Lower, Brian H.; Yongsunthon, Ruchirej; Shi, Liang; Wildling, Linda; Gruber, Hermann J.; Wigginton, Nicholas S.; Reardon, Catherine L.; Pinchuk, Grigoriy E.; Droubay, Timothy C.; Boily, Jean-François; Lower, Steven K.

doi:10.1128/aem.02108-08

Cited by 100 publications

(103 citation statements)

References 28 publications

(40 reference statements)

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“…oneidensis expresses the two outer membrane cytochromes MtrC and outer membrane cytochrome A (OmcA) under ferric iron-reducing conditions. In vitro evidence suggested that OmcA and MtrC build a high-affinity complex, but this in vitro finding is not supported by in vivo colocalization studies (47,85). The role of these outer membrane cytochromes in respiration does not seem to be interchangeable (85).…”

Section: Extracellular Electron Acceptorsmentioning

confidence: 74%

Dissimilatory Reduction of Extracellular Electron Acceptors in Anaerobic Respiration

Richter

Schicklberger

Gescher

2012

Appl Environ Microbiol

237

181

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An extension of the respiratory chain to the cell surface is necessary to reduce extracellular electron acceptors like ferric iron or manganese oxides. In the past few years, more and more compounds were revealed to be reduced at the surface of the outer membrane of Gram-negative bacteria, and the list does not seem to have an end so far. Shewanella as well as Geobacter strains are model organisms to discover the biochemistry that enables the dissimilatory reduction of extracellular electron acceptors. In both cases, c-type cytochromes are essential electron-transferring proteins. They make the journey of respiratory electrons from the cytoplasmic membrane through periplasm and over the outer membrane possible. Outer membrane cytochromes have the ability to catalyze the last step of the respiratory chains. Still, recent discoveries provided evidence that they are accompanied by further factors that allow or at least facilitate extracellular reduction. This review gives a condensed overview of our current knowledge of extracellular respiration, highlights recent discoveries, and discusses critically the influence of different strategies for terminal electron transfer reactions.

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Section: Extracellular Electron Acceptorsmentioning

confidence: 74%

Dissimilatory Reduction of Extracellular Electron Acceptors in Anaerobic Respiration

Richter

Schicklberger

Gescher

2012

Appl Environ Microbiol

237

181

View full text Add to dashboard Cite

show abstract

“…Previous studies on S. oneidensis used proteinase K susceptibility to demonstrate the cell-surface exposure of MtrC and OmcA (22). Analyses with immunogold localization and functionalized atomic force microscopy also showed the surface localization of MtrC and OmcA (15,23). Here, hybridization with gold-labeled MtrC antibodies demonstrated that MtrC also is exposed on the surface of the MtrCAB proteoliposomes (Fig.…”

Section: Topology Of Mtrcab In Proteoliposomesmentioning

confidence: 81%

Rapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals

White

Shi

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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184

209

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The mineral-respiring bacterium Shewanella oneidensis uses a protein complex, MtrCAB, composed of two decaheme cytochromes, MtrC and MtrA, brought together inside a transmembrane porin, MtrB, to transport electrons across the outer membrane to a variety of mineral-based electron acceptors. A proteoliposome system containing a pool of internalized electron carriers was used to investigate how the topology of the MtrCAB complex relates to its ability to transport electrons across a lipid bilayer to externally located Fe(III) oxides. With MtrA facing the interior and MtrC exposed on the outer surface of the phospholipid bilayer, the established in vivo orientation, electron transfer from the interior electron carrier pool through MtrCAB to solid-phase Fe(III) oxides was demonstrated. The rates were 10 3 times higher than those reported for reduction of goethite, hematite, and lepidocrocite by S. oneidensis, and the order of the reaction rates was consistent with those observed in S. oneidensis cultures. In contrast, established rates for single turnover reactions between purified MtrC and Fe(III) oxides were 10 3 times lower. By providing a continuous flow of electrons, the proteoliposome experiments demonstrate that conduction through MtrCAB directly to Fe(III) oxides is sufficient to support in vivo, anaerobic, solid-phase iron respiration.mineral respiration | multiheme cytochromes | proteoliposome

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“…The evidence that the conductive filaments were involved in extracellular electron transfer in Shewanella was the finding that deletion of the genes for the c-type cytochromes OmcA and MtrC, which are necessary for extracellular electron transfer, resulted in nonconductive filaments, suggesting that the cytochromes were associated with the filaments (7). However, subsequent studies specifically designed to localize these cytochromes revealed that, although the cytochromes were extracellular, they were attached to the cells or in the exopolymeric matrix and not aligned along the pili (24,25,30,40,43). Subsequent reviews of electron transfer to Fe(III) in Shewanella oneidensis (44,45) appear to have dropped the nanowire concept and focused on the first and second mechanisms.…”

mentioning

confidence: 99%

Alignment of the c -Type Cytochrome OmcS along Pili of Geobacter sulfurreducens

Leang

Qian

Mester

et al. 2010

Appl Environ Microbiol

315

263

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Antibody Recognition Force Microscopy Shows that Outer Membrane Cytochromes OmcA and MtrC Are Expressed on the Exterior Surface of Shewanella oneidensis MR-1

Cited by 100 publications

References 28 publications

Dissimilatory Reduction of Extracellular Electron Acceptors in Anaerobic Respiration

Dissimilatory Reduction of Extracellular Electron Acceptors in Anaerobic Respiration

Rapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals

Alignment of the c -Type Cytochrome OmcS along Pili of Geobacter sulfurreducens

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