Effect of specific trifluoroacetylation of individual cytochrome c lysines on the reaction with cytochrome oxidase
- PMID: 189807
- DOI: 10.1021/bi00623a007
Effect of specific trifluoroacetylation of individual cytochrome c lysines on the reaction with cytochrome oxidase
Abstract
We have prepared three different cytochrome c derivatives, each containing a single specifically trifluoroacetylated lysine at residues 13, 55, and 99, respectively. The only modification that affected cytochrome c oxidase (EC 1.9.3.1) activity was that of lysine-13 at the top of the heme crevice. Trifluoroacetylation of lysine-13 increased the apparent Michaelis constant fivefold compared to that of native cytochrome c, but did not affect the maximum velocity. Trifluoroacetylation of lysine-55 at the left side of the cytochrome c molecule did not affect cytochrome oxidase activity in any way, nor did trifluoroacetylation of lysine-99 at the rear of the cytochrome c molecule. This indicates that the cytochrome oxidase binding site on cytochrome c involved only the front of the cytochrome c molecule and those lysines immediately surrounding the heme crevice.
Similar articles
-
Use of specific lysine modifications to locate the reaction site of cytochrome c with cytochrome oxidase.Biochemistry. 1977 Nov 15;16(23):4971-4. doi: 10.1021/bi00642a005. Biochemistry. 1977. PMID: 199245
-
Use of specific trifluoroacetylation of lysine residues in cytochrome c to study the reaction with cytochrome b5, cytochrome c1, and cytochrome oxidase.Biochim Biophys Acta. 1980 Sep 5;592(2):303-13. doi: 10.1016/0005-2728(80)90191-7. Biochim Biophys Acta. 1980. PMID: 6250589
-
An enzyme kinetics and 19F nuclear magnetic resonance study of selectively trifluoroacetylated cytochrome c derivatives.Biochemistry. 1976 Jul 27;15(15):3198-205. doi: 10.1021/bi00660a007. Biochemistry. 1976. PMID: 182207
-
Structure of cytochrome c oxidase.Biochim Biophys Acta. 1983 Jul 15;726(2):135-48. doi: 10.1016/0304-4173(83)90003-4. Biochim Biophys Acta. 1983. PMID: 6307356 Review. No abstract available.
-
Cytochrome oxidase: some unsolved problems and controversial issues.Arch Biochem Biophys. 1990 Aug 1;280(2):233-41. doi: 10.1016/0003-9861(90)90325-s. Arch Biochem Biophys. 1990. PMID: 2164353 Review. No abstract available.
Cited by
-
Redox conformation changes in refined tuna cytochrome c.Proc Natl Acad Sci U S A. 1980 Nov;77(11):6371-5. doi: 10.1073/pnas.77.11.6371. Proc Natl Acad Sci U S A. 1980. PMID: 6256733 Free PMC article.
-
Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation.Cells. 2022 Dec 12;11(24):4014. doi: 10.3390/cells11244014. Cells. 2022. PMID: 36552779 Free PMC article.
-
Chemical modification of the haem propionate of cytochrome c. A re-evaluation of the reaction of cytochrome c with a water-soluble carbodi-imide.Biochem J. 1986 Nov 15;240(1):181-7. doi: 10.1042/bj2400181. Biochem J. 1986. PMID: 3030276 Free PMC article.
-
Evolution of cytochrome C investigated by the maximum parsimony method.J Mol Evol. 1981;17(4):197-213. doi: 10.1007/BF01732758. J Mol Evol. 1981. PMID: 6267311
-
Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chem Rev. 2014 Apr 23;114(8):4366-469. doi: 10.1021/cr400479b. Chem Rev. 2014. PMID: 24758379 Free PMC article. Review. No abstract available.