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• W1994489085 abstract "The final interprotein electron transfer (ET) in the mammalian respiratory chain, from cytochrome c (Cyt c ) to cytochrome c oxidase (C c O) is investigated by 1 H- 15 N heteronuclear single quantum coherence spectral analysis. The chemical shift perturbation in isotope-labeled Cyt c induced by addition of unlabeled C c O indicates that the hydrophobic heme periphery and adjacent hydrophobic amino acid residues of Cyt c dominantly contribute to the complex formation, whereas charged residues near the hydrophobic core refine the orientation of Cyt c to provide well controlled ET. Upon oxidation of Cyt c , the specific line broadening of N-H signals disappeared and high field 1 H chemical shifts of the N-terminal helix were observed, suggesting that the interactions of the N-terminal helix with C c O are reduced by steric constraint in oxidized Cyt c , while the chemical shift perturbations in the C-terminal helix indicate notable interactions of oxidized Cyt c with C c O. These results suggest that the overall affinity of oxidized Cyt c for C c O is significantly, but not very much weaker than that of reduced Cyt c . Thus, electron transfer is gated by dissociation of oxidized Cyt c from C c O, the rate of which is controlled by the affinity of oxidized Cyt c to C c O for providing an appropriate electron transfer rate for the most effective energy coupling. The conformational changes in Lys13 upon C c O binding to oxidized Cyt c , shown by 1 H- and 1 H, 15 N-chemical shifts, are also expected to gate intraprotein ET by a polarity control of heme c environment." @default.
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• W1994489085 date "2011-07-11" @default.
• W1994489085 modified "2023-10-16" @default.
• W1994489085 title "NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase" @default.
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• W1994489085 doi "https://doi.org/10.1073/pnas.1108320108" @default.
• W1994489085 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3145682" @default.
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