Site-Directedly Mutated Human Cytochrome c Which Retains Heme c via Only One Thioether Bond
- 30 June 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 108 (1) , 7-8
- https://doi.org/10.1093/oxfordjournals.jbchem.a123165
Abstract
Although Cys-14 (human numbering) of cytochrome c was conserved during its molecular evolution and it is supposed to be essential for most cytochromes c to retain heme c via two thioether bonds, a site-directedly mutated human cytochrome c which has an alanine residue at this position and only one thioether bond through Cys-17 turns out to be functional. This shows that Cys-14 is not essential. The absorption spectrum of the atypical cytochrome c is red shifted, and similar to those of Euglena and Crithidia cytochromes c, which also have only one thioether bond [Pettigrew, G.W., Leaver, J.L., Meyer, T.E., & Ryle, A.P. (1975) Biochenm. J. 147, 291–302].This publication has 12 references indexed in Scilit:
- Expression and activity of a gene encoding rat cytochrome c in the yeast Saccharomyces cerevisiaeGene, 1989
- Molecular Cloning and Nucleotide Sequence of a cDNA Encoding Euglena gracilis Cytochrome C11The Journal of Biochemistry, 1989
- Replacements of lysine 32 in yeast cytochrome c. Effects on the binding and reactivity with physiological partners.Journal of Biological Chemistry, 1988
- Amino Acid Replacement Studies of Human Cytochrome c by a Complementation System Using CYC1 Deficient YeastThe Journal of Biochemistry, 1988
- Construction of a Human Cytochrome c Gene and Its Functional Expression in Saccharomyces cerevisiaeThe Journal of Biochemistry, 1988
- Replacement of the invariant lysine 77 by arginine in yeast iso-1-cytochrome c results in enhanced and normal activities in vitro and in vivo.Journal of Biological Chemistry, 1987
- Functional expression of rat cytochrome c in Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences, 1986
- Amino acid replacements in yeast iso-1-cytochrome c. Comparison with the phylogenetic series and the tertiary structure of related cytochromes c.Journal of Biological Chemistry, 1986
- Substitutions of proline 76 in yeast iso-1-cytochrome c. Analysis of residues compatible and incompatible with folding requirements.Journal of Biological Chemistry, 1985
- Primary site and second site revertants of missense mutants of the evolutionarily invariant tryptophan 64 in iso-1-cytochrome c from yeast.Journal of Biological Chemistry, 1979