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Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b 5


Biochemistry 16(23): 4975-4978
Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b 5
The rate of reduction of [horse heart] cytochrome c by [beef] liver microsomal cytochrome b5 was found to be strongly inhibited by high ionic strength, indicating that the reaction probably involves complementary charge interactions between positively charged lysine groups on cytochrome c and negatively charged carboxyl groups on cytochrome b5. The reaction rates between cytochrome b5 and cytochrome c derivatives modified at single lysine residues to form trifluoroacetylated or trifluoromethylphenylcarbamoylated lysines were studied to determine the role of individual lysines in the reaction. The only modifications that decreased the reaction rate were those of lysines immediately surrounding the heme crevice, lysines 8, 13, 25, 27, 72 and 79. Modification of lysines 22, 55, 99 and 100 had no effect on the rate. Lysines 13, 25, 27, 72 and 79 of cytochrome c form complementary charge interactions with the cytochrome b5 carboxyl groups Asp-48, Glu-43, Glu-44, Asp-60 and the most exposed heme propionate, respectively. The same modifications that affect the cytochrome b5 activity also affect the cytochrome oxidase activity of cytochrome c, indicating that the pattern of complementary charge interactions is rather similar for the 2 complexes.

Accession: 005254621

PMID: 199233

DOI: 10.1021/bi00642a006

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Related references

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