doi: 10.1073/pnas.76.12.6132.
Electron-nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase: identification of the free radical site with a methionyl cluster
- PMID: 230500
- PMCID: PMC411817
- DOI: 10.1073/pnas.76.12.6132
Item in Clipboard
Electron-nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase: identification of the free radical site with a methionyl cluster
Proc Natl Acad Sci U S A.
1979 Dec.
Abstract
The results of electron-nuclear double resonance and electron paramagnetic resonance (EPR) studies on the hydrogen peroxide compound of yeast cytochrome c peroxidase are inconsistent with previous proposals for the source of the EPR signal in this compound, in particular with its identification with an aromatic amino acid radical such as would arise by oxidation of a tryptophanyl side chain. The present observations lead us to propose that the EPR signal is associated with a cluster containing at least one methionine and in which proximate side chains share the charge created by loss of one electron.
Similar articles
-
Studies of the radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis.Proc Natl Acad Sci U S A. 1986 Mar;83(5):1295-9. doi: 10.1073/pnas.83.5.1295. Proc Natl Acad Sci U S A. 1986. PMID: 3006043 Free PMC article.
-
Electron paramagnetic and electron nuclear double resonance of the hydrogen peroxide compound of cytochrome c peroxidase.J Biol Chem. 1981 Jul 10;256(13):6556-64. J Biol Chem. 1981. PMID: 6263919
-
Compound I radical in site-directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron-nuclear double resonance.Biochemistry. 1991 Feb 19;30(7):1986-96. doi: 10.1021/bi00221a036. Biochemistry. 1991. PMID: 1847080
-
Control of the transfer of oxidizing equivalents between heme iron and free radical site in yeast cytochrome c peroxidase.J Biol Chem. 1983 Apr 10;258(7):4356-63. J Biol Chem. 1983. PMID: 6300084
-
Tryptophan or tyrosine? On the nature of the amino acid radical formed following hydrogen peroxide treatment of cytochrome c oxidase.Biochim Biophys Acta. 2004 Apr 12;1655(1-3):372-80. doi: 10.1016/j.bbabio.2003.06.006. Biochim Biophys Acta. 2004. PMID: 15100053 Review.
Cited by
-
Studies of the radical species in compound ES of cytochrome c peroxidase altered by site-directed mutagenesis.Proc Natl Acad Sci U S A. 1986 Mar;83(5):1295-9. doi: 10.1073/pnas.83.5.1295. Proc Natl Acad Sci U S A. 1986. PMID: 3006043 Free PMC article.
-
The Rise of Radicals in Bioinorganic Chemistry.Isr J Chem. 2016 Oct;56(9-10):640-648. doi: 10.1002/ijch.201600069. Epub 2016 Jul 29. Isr J Chem. 2016. PMID: 28239191 Free PMC article.
-
Copper electron-nuclear double resonance of cytochrome c oxidase.Proc Natl Acad Sci U S A. 1980 Mar;77(3):1452-6. doi: 10.1073/pnas.77.3.1452. Proc Natl Acad Sci U S A. 1980. PMID: 6246493 Free PMC article.
-
Heme enzyme structure and function.Chem Rev. 2014 Apr 9;114(7):3919-62. doi: 10.1021/cr400415k. Epub 2014 Jan 8. Chem Rev. 2014. PMID: 24400737 Free PMC article. Review. No abstract available.
-
A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase.Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):11118-22. doi: 10.1073/pnas.91.23.11118. Proc Natl Acad Sci U S A. 1994. PMID: 7972020 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
