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- W2078646902 abstract "The binding of methionine to one of the axial positions of the heme iron in various modified mammalian-type cytochromes c has been studied by nuclear magnetic resonance spectroscopy. The modifications of the protein included formylation of tryptophan, alkylation of methionine, and polymerization by treatment with ethanol. Comparison of the data on methionine coordination with data on the ability of the modified cytochromes c to restore the respiration of cytochrome c-depleted rat liver mitochondria, indicates that the redox carrier properties of cytochrome c are maintained only if methionine is bound to the heme iron in the oxidized and the reduced form." @default.
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- W2078646902 date "1971-11-01" @default.
- W2078646902 modified "2023-09-25" @default.
- W2078646902 title "Structural studies of modified cytochromes c by nuclear magnetic resonance spectroscopy" @default.
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- W2078646902 doi "https://doi.org/10.1016/0005-2728(71)90237-4" @default.
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