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• W2078559967 abstract "The association of the tryptic fragment of bovine microsomal cytochrome b 5 with cytochrome c has been studied by one‐ and two‐dimensional 1 H‐NMR spectroscopy. The association of cytochromes to form protein complexes is apparent from the increase in linewidths for resonances of ferricytochrome b 5 as well as small perturbations in their chemical shifts that occur upon increasing the cytochrome c/b 5 molar ratio. The changes in the chemical shifts of hyperfine shifted resonances of ferricytochrome b 5 with increasing ratios of ferricytochrome c indicate the formation of binary 1:1 complexes and ternary 1:2 complexes. Similarly, titrations of the linewidth of resolved resonances of ferricytochrome b 5 are consistent with stoichiometries of 1:1 and 1:2 for complexes formed between cytochromes b 5 and c . Surprisingly, in the 1:1 complex, mobility is shown to be a function of ionic strength. Two‐dimensional correlated spectroscopy (COSY) and nuclear Overhauser enhancement spectroscopy (NOESY) of the binary complex formed between ferricytochrome b 5 and c indicate that the positions of many resonances attributable to amino acids are unaltered by protein association, although distinctive chemical shift changes are detected in the α‐CH of the haem C17 propionate. The protein complex detected by NMR is discussed with respect to the model for the binary complex proposed by Salemme and possible mechanisms of electron transfer." @default.
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• W2078559967 date "1990-09-01" @default.
• W2078559967 modified "2023-10-17" @default.
• W2078559967 title "The formation of protein complexes between ferricytochrome <i>b</i>₅ and ferricytochrome <i>c</i> studied using high‐resolution ¹H‐NMR spectroscopy" @default.
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• W2078559967 doi "https://doi.org/10.1111/j.1432-1033.1990.tb19281.x" @default.
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