ArticleThe journal of physical chemistry. B2011
Solution-based structural analysis of the decaheme cytochrome, MtrA, by small-angle X-ray scattering and analytical ultracentrifugation.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Recent Advances in Analytical Platform for Single-Cell Microbial Electrochemistry.Chemical & biomedical imaging · 2026Review
- Conductive proteins-based extracellular electron transfer of electroactive microorganisms.Quantitative biology (Beijing, China) · 2023Review
- Article
- Thermophiles; or, the Modern Prometheus: The Importance of Extreme Microorganisms for Understanding and Applying Extracellular Electron Transfer.Frontiers in microbiology · 2019Article
- Structural modeling of an outer membrane electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic redox partners.The Journal of biological chemistry · 2018Article
- Ultrastructure ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Impedance spectroscopy of single bacterial nanofilament reveals water-mediated charge transfer.PloS one · 2018Article
- A Synthetic Biology Approach to Engineering Living Photovoltaics.Energy & environmental science · 2017Article
- Comparative Genomic Analysis of Neutrophilic Iron(II) Oxidizer Genomes for Candidate Genes in Extracellular Electron Transfer.Frontiers in microbiology · 2017Article
- Allosteric Inhibition of Human Ribonucleotide Reductase by dATP Entails the Stabilization of a Hexamer.Biochemistry · 2016Article
- Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities.Journal of the Royal Society, Interface · 2015Review
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Genomic analyses of bacterial porin-cytochrome gene clusters.Frontiers in microbiology · 2014Article
- 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
- Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family.Biochemical Society transactions · 2012Review
- Characterization of axial and proximal histidine mutations of the decaheme cytochrome MtrA from Shewanella sp. strain ANA-3 and implications for the electron transport system.Journal of bacteriology · 2012Article
- Reconstruction of Extracellular Respiratory Pathways for Iron(III) Reduction in Shewanella Oneidensis Strain MR-1.Frontiers in microbiology · 2012Article
- Molecular Underpinnings of Fe(III) Oxide Reduction by Shewanella Oneidensis MR-1.Frontiers in microbiology · 2012Article
- Multi-heme proteins: nature's electronic multi-purpose tool.Biochimica et biophysica actaReview
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
The potential exploitation of metal-reducing bacteria as a means for environmental cleanup or alternative fuel is an exciting prospect; however, the cellular processes that would allow for these applications need to be better understood. MtrA is a periplasmic decaheme c-type cytochrome from Shewanella oneidensis involved in the reduction of extracellular iron oxides and therefore is a critical element in Shewanella ability to engage in extracellular charge transfer. As a relatively small 333-residue protein, the heme content is surprisingly high. MtrA is believed to obtain electrons from the inner membrane-bound quinol oxidoreductase, CymA, and shuttle them across the outer membrane to MtrC, another decaheme cytochrome that directly interacts with insoluble metal oxides. How MtrA is able to perform this task is a question of interest. Here through the use of two solution-based techniques, small-angle X-ray scattering (SAXS) and analytical ultracentrifugation (AUC), we present the first structural analysis of MtrA. Our results establish that between 0.5 and 4 mg/mL, MtrA exists as a monomeric protein that is shaped like an extended molecular "wire" with a maximum protein dimension (D(max)) of 104 Å and a rod-like aspect ratio of 2.2 to 2.5. This study contributes to a greater understanding of how MtrA fulfills its role in the redox processes that must occur before electrons reach the outside of the cell.
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