ArticleBiophysical journal2010
The molecular determinants of the increased reduction potential of the rubredoxin domain of rubrerythrin relative to rubredoxin.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Predicting Metalloprotein Redox Potentials with Machine Learning: A Focus on Iron-Sulfur Systems.Journal of chemical information and modeling · 2025Article
- Benchmark Study of Redox Potential Calculations for Iron-Sulfur Clusters in Proteins.Inorganic chemistry · 2022Article
- Mitochondrial iron-sulfur clusters: Structure, function, and an emerging role in vascular biology.Redox biology · 2021Review
- The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductase.Scientific reports · 2018Article
- Structural-functional analysis of engineered protein-nanoparticle assemblies using graphene microelectrodes.Chemical science · 2017Article
- Web-based computational chemistry education with CHARMMing III: Reduction potentials of electron transfer proteins.PLoS computational biology · 2014Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Calculating standard reduction potentials of [4Fe-4S] proteins.Journal of computational chemistry · 2013Article
- Characterizing the effects of the protein environment on the reduction potentials of metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Desulforubrerythrin from Campylobacter jejuni, a novel multidomain protein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
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5 authors at 2 institutions in 1 country.
Funding
Abstract
Based on the crystal structures, three possible sequence determinants have been suggested as the cause of a 285 mV increase in reduction potential of the rubredoxin domain of rubrerythrin over rubredoxin by modulating the polar environment around the redox site. Here, electrostatic calculations of crystal structures of rubredoxin and rubrerythrin and molecular dynamics simulations of rubredoxin wild-type and mutants are used to elucidate the contributions to the increased reduction potential. Asn(160) and His(179) in rubrerythrin versus valines in rubredoxins are predicted to be the major contributors, as the polar side chains contribute significantly to the electrostatic potential in the redox site region. The mutant simulations show both side chains rotating on a nanosecond timescale between two conformations with different electrostatic contributions. Reduction also causes a change in the reduction energy that is consistent with a linear response due to the interesting mechanism of shifting the relative populations of the two conformations. In addition to this, a simulation of a triple mutant indicates the side-chain rotations are approximately anticorrelated so whereas one is in the high potential conformation, the other is in the low potential conformation. However, Ala(176) in rubrerythrin versus a leucine in rubredoxin is not predicted to be a large contributor, because the solvent accessibility increases only slightly in mutant simulations and because it is buried in the interface of the rubrerythrin homodimer.
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