ArticleFrontiers in microbiology2015
Characterization of MtoD from Sideroxydans lithotrophicus: a cytochrome c electron shuttle used in lithoautotrophic growth.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- Deciphering the Mto electron uptake pathway ofApplied and environmental microbiology · 2026Article
- Modeling neutrophilic iron-oxidizing bacteria: a KBase narrative resource describing newly integrated metabolic reactions.Microbiology resource announcements · 2026Article
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- Microbial magnetite oxidation via MtoAB porin-multiheme cytochrome complex inApplied and environmental microbiology · 2025Article
- 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
- Genetic Code Expansion inACS synthetic biology · 2024Article
- Development of an efficient, effective, and economical technology for proteome analysis.Cell reports methods · 2024Article
- Gallionellaceae pangenomic analysis reveals insight into phylogeny, metabolic flexibility, and iron oxidation mechanisms.mSystems · 2023Article
- Conductive proteins-based extracellular electron transfer of electroactive microorganisms.Quantitative biology (Beijing, China) · 2023Review
- Microbe-driven elemental cycling enables microbial adaptation to deep-sea ferromanganese nodule sediment fields.Microbiome · 2023Article
- Light-driven ammonium oxidation to dinitrogen gas by self-photosensitized biohybrid anammox systems.iScience · 2023Article
- Mixotrophy broadens the ecological niche range of the iron oxidizer Sideroxydans sp. CL21 isolated from an iron-rich peatland.FEMS microbiology ecology · 2023Article
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- Electroactive biofilms: how microbial electron transfer enables bioelectrochemical applications.Journal of industrial microbiology & biotechnology · 2022Review
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- Computational structure prediction provides a plausible mechanism for electron transfer by the outer membrane protein Cyc2 from Acidithiobacillus ferrooxidans.Protein science : a publication of the Protein Society · 2021Article
- An evolving view on biogeochemical cycling of iron.Nature reviews. Microbiology · 2021Review
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- Microbial electro-fermentation for synthesis of chemicals and biofuels driven by bi-directional extracellular electron transfer.Synthetic and systems biotechnology · 2020Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The autotrophic Sideroxydans lithotrophicus ES-1 can grow by coupling the oxidation of ferrous iron to the reduction of oxygen. Soluble ferrous iron is oxidized at the surface of the cell by an MtoAB porin-cytochrome complex that functions as an electron conduit through the outer membrane. Electrons are then transported to the cytoplasmic membrane where they are used to generate proton motive force (PMF) (for ATP synthesis) and NADH for autotrophic processes such as carbon fixation. As part of the mtoAB gene cluster, S. lithotrophicus also contains the gene mtoD that is proposed to encode a cytochrome c protein. We isolated mtoD from a Shewanella oneidensis expression system where the mtoD gene was expressed on a pBAD plasmid vector. Biochemical, biophysical, and crystallographic characterization of the purified MtoD revealed it as an 11 kDa monomeric protein containing a single heme. Sequence and structural alignment indicated that MtoD belonged to the class-1 cytochrome c family and had a similar fold to ferricytochrome c552 family, however the MtoD heme is bis-histidine coordinated and is substantially more exposed than the hemes of other family members. The reduction potential of the MtoD heme at pH 7 was +155 mV vs. Standard Hydrogen Electrode, which is approximately 100 mV lower than that of mitochondrial cytochrome c. Consideration of the properties of MtoD in the context of the potential respiratory partners identified from the genome suggests that MtoD could associate to multiple electron transfer partners as the primary periplasmic electron shuttle.
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