ArticleJournal of bacteriology2007
Specific bonds between an iron oxide surface and outer membrane cytochromes MtrC and OmcA from Shewanella oneidensis MR-1.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 138 citations in OpenAlex.
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- Bacterial extracellular electron transfer: a powerful route to the green biosynthesis of inorganic nanomaterials for multifunctional applications.Journal of nanobiotechnology · 2021Review
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- Outer MembraneApplied and environmental microbiology · 2020Article
- FeGenie: A Comprehensive Tool for the Identification of Iron Genes and Iron Gene Neighborhoods in Genome and Metagenome Assemblies.Frontiers in microbiology · 2020Article
- FeRSC advances · 2019Article
- Whole-cell circular dichroism difference spectroscopy reveals an in vivo-specific deca-heme conformation in bacterial surface cytochromes.Chemical communications (Cambridge, England) · 2018Article
- Effects of Copper Oxide Nanoparticles on Paddy Soil Properties and Components.Nanomaterials (Basel, Switzerland) · 2018Article
- Proton Transport in the Outer-Membrane Flavocytochrome Complex Limits the Rate of Extracellular Electron Transport.Angewandte Chemie (International ed. in English) · 2017Article
- Extracellular electron transfer mechanisms between microorganisms and minerals.Nature reviews. Microbiology · 2016Review
- A Re-evaluation of Electron-Transfer Mechanisms in Microbial Electrochemistry:ChemElectroChem · 2016Article
- Modelling extracellular limitations for mediated versus direct interspecies electron transfer.The ISME journal · 2016Article
- Cation-limited kinetic model for microbial extracellular electron transport via an outer membrane cytochromeBiophysics and physicobiology · 2016Review
- Transcriptional mechanisms for differential expression of outer membrane cytochrome genes omcA and mtrC in Shewanella oneidensis MR-1.BMC microbiology · 2015Article
- Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities.Journal of the Royal Society, Interface · 2015Review
- Catabolic and regulatory systems in Shewanella oneidensis MR-1 involved in electricity generation in microbial fuel cells.Frontiers in microbiology · 2015Review
- Modeling biofilms with dual extracellular electron transfer mechanisms.Physical chemistry chemical physics : PCCP · 2013Article
- Rapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Promotion of iron oxide reduction and extracellular electron transfer in Shewanella oneidensis by DMSO.PloS one · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shewanella oneidensis MR-1 is purported to express outer membrane cytochromes (e.g., MtrC and OmcA) that transfer electrons directly to Fe(III) in a mineral during anaerobic respiration. A prerequisite for this type of reaction would be the formation of a stable bond between a cytochrome and an iron oxide surface. Atomic force microscopy (AFM) was used to detect whether a specific bond forms between a hematite (Fe(2)O(3)) thin film, created with oxygen plasma-assisted molecular beam epitaxy, and recombinant MtrC or OmcA molecules coupled to gold substrates. Force spectra displayed a unique force signature indicative of a specific bond between each cytochrome and the hematite surface. The strength of the OmcA-hematite bond was approximately twice that of the MtrC-hematite bond, but direct binding to hematite was twice as favorable for MtrC. Reversible folding/unfolding reactions were observed for mechanically denatured MtrC molecules bound to hematite. The force measurements for the hematite-cytochrome pairs were compared to spectra collected for an iron oxide and S. oneidensis under anaerobic conditions. There is a strong correlation between the whole-cell and pure-protein force spectra, suggesting that the unique binding attributes of each cytochrome complement one another and allow both MtrC and OmcA to play a prominent role in the transfer of electrons to Fe(III) in minerals. Finally, by comparing the magnitudes of binding force for the whole-cell versus pure-protein data, we were able to estimate that a single bacterium of S. oneidensis (2 by 0.5 microm) expresses approximately 10(4) cytochromes on its outer surface.
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