ArticleFrontiers in microbiology2012
Identification and Characterization of MtoA: A Decaheme c-Type Cytochrome of the Neutrophilic Fe(II)-Oxidizing Bacterium Sideroxydans lithotrophicus ES-1.
Article in Frontiers in microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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91 citing papers in PubMed.
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- Comparative transcriptomics and scarless genome editing uncover a periplasmicApplied and environmental microbiology · 2026Article
- Metabolic diversity of Ferrovaceae and potential contributions to iron oxidation.Applied and environmental microbiology · 2026Article
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- Modeling neutrophilic iron-oxidizing bacteria: a KBase narrative resource describing newly integrated metabolic reactions.Microbiology resource announcements · 2026Article
- An organotrophicApplied and environmental microbiology · 2025Article
- Microbial magnetite oxidation via MtoAB porin-multiheme cytochrome complex inApplied and environmental microbiology · 2025Article
- High diversity of nitrifying bacteria and archaea in biofilms from a subsea tunnel.FEMS microbiology ecology · 2025Article
- Electron transfer in multicentre redox proteins: from fundamentals to extracellular electron transfer.Bioscience reports · 2025Review
- Microbial magnetite oxidation via MtoAB porin-multiheme cytochrome complex inbioRxiv : the preprint server for biology · 2025Article
- Resonance assignments of cytochrome MtoD from the extracellular electron uptake pathway of sideroxydans lithotrophicus ES-1.Biomolecular NMR assignments · 2024Article
- Microbial acidification by N, S, Fe and Mn oxidation as a key mechanism for deterioration of subsea tunnel sprayed concrete.Scientific reports · 2024Article
- Article
- MmcA is an electron conduit that facilitates both intracellular and extracellular electron transport in Methanosarcina acetivorans.Nature communications · 2024Article
- Gallionellaceae in rice root plaque: metabolic roles in iron oxidation, nutrient cycling, and plant interactions.Applied and environmental microbiology · 2023Article
- Gallionellaceae pangenomic analysis reveals insight into phylogeny, metabolic flexibility, and iron oxidation mechanisms.mSystems · 2023Article
- Proterozoic Acquisition of Archaeal Genes for Extracellular Electron Transfer: A Metabolic Adaptation of Aerobic Ammonia-Oxidizing Bacteria to Oxygen Limitation.Molecular biology and evolution · 2023Article
- MmcA is an electron conduit that facilitates both intracellular and extracellular electron transport inbioRxiv : the preprint server for biology · 2023Article
- Mixotrophy broadens the ecological niche range of the iron oxidizer Sideroxydans sp. CL21 isolated from an iron-rich peatland.FEMS microbiology ecology · 2023Article
31 more citing papers are in PubMed but not listed here.
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Abstract
The Gram-negative bacterium Sideroxydans lithotrophicus ES-1 (ES-1) grows on FeCO(3) or FeS at oxic-anoxic interfaces at circumneutral pH, and the ES-1-mediated Fe(II) oxidation occurs extracellularly. However, the molecular mechanisms underlying ES-1's ability to oxidize Fe(II) remain unknown. Survey of the ES-1 genome for candidate genes for microbial extracellular Fe(II) oxidation revealed that it contained a three-gene cluster encoding homologs of Shewanella oneidensis MR-1 (MR-1) MtrA, MtrB, and CymA that are involved in extracellular Fe(III) reduction. Homologs of MtrA and MtrB were also previously shown to be involved in extracellular Fe(II) oxidation by Rhodopseudomonas palustris TIE-1. To distinguish them from those found in MR-1, the identified homologs were named MtoAB and CymA(ES-1). Cloned mtoA partially complemented an MR-1 mutant without MtrA with regards to ferrihydrite reduction. Characterization of purified MtoA showed that it was a decaheme c-type cytochrome and oxidized soluble Fe(II). Oxidation of Fe(II) by MtoA was pH- and Fe(II)-complexing ligand-dependent. Under conditions tested, MtoA oxidized Fe(II) from pH 7 to pH 9 with the optimal rate at pH 9. MtoA oxidized Fe(II) complexed with different ligands at different rates. The reaction rates followed the order Fe(II)Cl(2) > Fe(II)-citrate > Fe(II)-NTA > Fe(II)-EDTA with the second-order rate constants ranging from 6.3 × 10(-3) μM(-1) s(-1) for oxidation of Fe(II)Cl(2) to 1.0 × 10(-3) μM(-1) s(-1) for oxidation of Fe(II)-EDTA. Thermodynamic modeling showed that redox reaction rates for the different Fe(II)-complexes correlated with their respective estimated reaction-free energies. Collectively, these results demonstrate that MtoA is a functional Fe(II)-oxidizing protein that, by working in concert with MtoB and CymA(ES-1), may oxidize Fe(II) at the bacterial surface and transfer released electrons across the bacterial cell envelope to the quinone pool in the inner membrane during extracellular Fe(II) oxidation by ES-1.
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