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• W2040973863 startingPage "8637" @default.
• W2040973863 abstract "The heme group in paramagnetic ( S = 1/2) ferricytochromes c typically displays a markedly asymmetric distribution of unpaired electron spin density among the heme pyrrole β substituents. This asymmetry is determined by the orientations of the heme axial ligands, histidine and methionine. One exception to this is ferricytochrome c 552 from Hydrogenobacter thermophilus , which has similar amounts of unpaired electron spin density at the β substituents on all four heme pyrroles. Here, determination of the orientation of the magnetic axes and analysis of NMR line shapes for H. thermophilus ferricytochrome c 552 is performed. These data reveal that the unusual electronic structure for this protein is a result of fluxionality of the heme axial methionine. It is proposed that the ligand undergoes inversion at the pyramidal sulfur, and the rapid interconversion between two diastereomeric forms results in the unusual heme electronic structure. Thus a fluxional process for a metal-bound amino acid side chain has now been identified." @default.
• W2040973863 created "2016-06-24" @default.
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• W2040973863 date "2004-05-25" @default.
• W2040973863 modified "2023-10-02" @default.
• W2040973863 title "Heme axial methionine fluxionality in <i>Hydrogenobacter thermophilus</i> cytochrome <i>c</i> ₅₅₂" @default.
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• W2040973863 doi "https://doi.org/10.1073/pnas.0402033101" @default.
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• W2040973863 hasPublicationYear "2004" @default.
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