ArticleProtein science : a publication of the Protein Society2021
Computational structure prediction provides a plausible mechanism for electron transfer by the outer membrane protein Cyc2 from Acidithiobacillus ferrooxidans.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 26 citations in OpenAlex.
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- Isolation, Sphalerite Bioleaching, and Whole Genome Sequencing ofLife (Basel, Switzerland) · 2025Article
- Vibrio natriegens as a superior host for the production of c-type cytochromes and difficult-to-express redox proteins.Scientific reports · 2024Article
- Electrochemical and structural characterization of recombinant respiratory proteins of the acidophilic iron oxidizerFrontiers in microbiology · 2024Article
- Metagenomic Features Characterized with Microbial Iron Oxidoreduction and Mineral Interaction in Southwest Indian Ridge.Microbiology spectrum · 2022Article
- Progress in bioleaching: fundamentals and mechanisms of microbial metal sulfide oxidation - part A.Applied microbiology and biotechnology · 2022Review
- 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
- Ferric Iron Reduction in Extreme Acidophiles.Frontiers in microbiology · 2021Review
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3 authors at 2 institutions in 1 country.
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Abstract
Cyc2 is the key protein in the outer membrane of Acidithiobacillus ferrooxidans that mediates electron transfer between extracellular inorganic iron and the intracellular central metabolism. This cytochrome c is specific for iron and interacts with periplasmic proteins to complete a reversible electron transport chain. A structure of Cyc2 has not yet been characterized experimentally. Here we describe a structural model of Cyc2, and associated proteins, to highlight a plausible mechanism for the ferrous iron electron transfer chain. A comparative modeling protocol specific for trans membrane beta barrel (TMBB) proteins in acidophilic conditions (pH ~ 2) was applied to the primary sequence of Cyc2. The proposed structure has three main regimes: Extracellular loops exposed to low-pH conditions, a TMBB, and an N-terminal cytochrome-like region within the periplasmic space. The Cyc2 model was further refined by identifying likely iron and heme docking sites. This represents the first computational model of Cyc2 that accounts for the membrane microenvironment and the acidity in the extracellular matrix. This approach can be used to model other TMBBs which can be critical for chemolithotrophic microbial growth.
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