ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2010
The effect of detergents and lipids on the properties of the outer-membrane protein OmcA from Shewanella oneidensis.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- Electron transfer in multicentre redox proteins: from fundamentals to extracellular electron transfer.Bioscience reports · 2025Review
- Deciphering Molecular Factors That Affect Electron Transfer at the Cell Surface of Electroactive Bacteria: The Case of OmcA fromMicroorganisms · 2022Article
- Observation of dielectric universalities in albumin, cytochrome C and Shewanella oneidensis MR-1 extracellular matrix.Scientific reports · 2017Article
- Exploring the molecular mechanisms of electron shuttling across the microbe/metal space.Frontiers in microbiology · 2014Article
- Molecular Underpinnings of Fe(III) Oxide Reduction by Shewanella Oneidensis MR-1.Frontiers in microbiology · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The protein OmcA from the bacterium Shewanella oneidensis was purified to homogeneity, and characterized using UV-vis spectroelectrochemistry, EPR, and circular dichroism (far- and near-UV regions). EPR spectroscopy showed that many different c-type hemes are present in the protein: high-spin, low-spin, and highly anisotropic low-spin hemes were all detected. The protein was shown to bind tightly to artificial membranes (liposomes) composed of dioleoylphosphatidylglycerol and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (60:40 molar ratio), which mimic the natural environment. However, on the basis of the spectroscopic and electrochemical studies, binding to liposomes does not appear to significantly alter either the structure or the properties of OmcA. On the other hand, the electrochemical properties of OmcA are noticeably changed in the presence of the detergents used during the initial purification stages. In particular, the reduction potentials of two out of the ten OmcA hemes appear to shift in the presence of detergent, perhaps because these hemes are solvent-exposed.
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