ReviewBiochemical Society transactions2012
Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family.
Review in Biochemical Society transactions, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 1 citations in OpenAlex.
- Metabolic diversity of Ferrovaceae and potential contributions to iron oxidation.Applied and environmental microbiology · 2026Article
- Electrogenic CH4 oxidation on a bioanode: putative extracellular electron transport system in Methylobacter sp.FEMS microbiology ecology · 2026Article
- Single-cell phenotyping of extracellular electron transfer via microdroplet encapsulation.Applied and environmental microbiology · 2025Article
- Electron transfer in multicentre redox proteins: from fundamentals to extracellular electron transfer.Bioscience reports · 2025Review
- Isolation and genomic analysis of "Applied and environmental microbiology · 2024Article
- Single-Cell Phenotyping of Extracellular Electron Transfer via Microdroplet Encapsulation.bioRxiv : the preprint server for biology · 2024Article
- Article
- Novel Microbial Groups Drive Productivity in an Archean Iron Formation.Frontiers in microbiology · 2021Article
- Genomic sequence analysis ofMicrobial genomics · 2020Article
- Direct Extracellular Electron Transfer of theBioMed research international · 2019Article
- Rapid construction of a whole-genome transposon insertion collection for Shewanella oneidensis by Knockout Sudoku.Nature communications · 2016Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Promotion of iron oxide reduction and extracellular electron transfer in Shewanella oneidensis by DMSO.PloS one · 2013Article
- Multi-heme proteins: nature's electronic multi-purpose tool.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Shewanella oneidensis MR-1 has the ability to use many external terminal electron acceptors during anaerobic respiration, such as DMSO. The pathway that facilitates this electron transfer includes the decahaem cytochrome DmsE, a paralogue of the MtrA family of decahaem cytochromes. Although both DmsE and MtrA are decahaem cytochromes implicated in the long-range electron transfer across a ~300 Å (1 Å=0.1 nm) wide periplasmic 'gap', MtrA has been shown to be only 105 Å in maximal length. In the present paper, DmsE is further characterized via protein film voltammetry, revealing that the electrochemistry of the DmsE haem cofactors display macroscopic potentials lower than those of MtrA by 100 mV. It is possible this tuning of the redox potential of DmsE is required to shuttle electrons to the outer-membrane proteins specific to DMSO reduction. Other decahaem cytochromes found in S. oneidensis, such as the outer-membrane proteins MtrC, MtrF and OmcA, have been shown to have electrochemical properties similar to those of MtrA, yet possess a different evolutionary relationship.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.