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• W2065598879 endingPage "15728" @default.
• W2065598879 startingPage "15720" @default.
• W2065598879 abstract "Analysis of NMR spectra reveals that the heme axial Met ligand orientation and dynamics in Nitrosomonas europaea cytochrome c552 (Ne cyt c) are dependent on the heme redox state. In the oxidized state, the heme axial Met is fluxional, interconverting between two conformers related to each other by inversion through the Met δS atom. In the reduced state, there is no evidence of fluxionality, with the Met occupying one conformation similar to that seen in the homologous Pseudomonas aeruginosa cytochrome c551. Comparison of the observed and calculated pseudocontact shifts for oxidized Ne cyt c using the reduced protein structure as a reference structure reveals a redox-dependent change in the structure of the loop bearing the axial Met (loop 3). Analysis of nuclear Overhauser effects (NOEs) and existing structural data provides further support for the redox state dependence of the loop 3 structure. Implications for electron transfer function are discussed." @default.
• W2065598879 created "2016-06-24" @default.
• W2065598879 creator A5009513269 @default.
• W2065598879 creator A5077328828 @default.
• W2065598879 date "2013-08-20" @default.
• W2065598879 modified "2023-10-16" @default.
• W2065598879 title "Redox State Dependence of Axial Ligand Dynamics in <i>Nitrosomonas europaea</i> Cytochrome <i>c</i>₅₅₂" @default.
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• W2065598879 doi "https://doi.org/10.1021/jp4064577" @default.
• W2065598879 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3865231" @default.
• W2065598879 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23909651" @default.
• W2065598879 hasPublicationYear "2013" @default.
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