Journal
FEBS LETTERS
Volume 587, Issue 14, Pages 2214-2218Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2013.05.047
Keywords
Oxidative stress; Reactive oxygen species; Microbial metabolism; Respiratory chain; Bacteria-host interaction; Hemeprotein
Funding
- Russian Foundation for Basic Research [11-04-00031-a]
- Ministero dell'Istruzione, dell'Universita e della Ricerca of Italy [FIRB RBFR08F41U_001, FIRB RBIN06E9Z8, PRIN 20107Z8XBW_005]
- FEBS
- Consiglio Nazionale delle Ricerche of Italy
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Cytochrome bd oxygen reductase from Escherichia coli has three hemes, b(558), b(595) and d. We found that the enzyme, as-prepared or in turnover with O-2, rapidly decomposes H2O2 with formation of approximately half a mole of O-2 per mole of H2O2. Such catalase activity vanishes upon cytochrome bd reduction, does not compete with the oxygen-reductase activity, is insensitive to NO, CO, antimycin-A and N-ethylmaleimide (NEM), but is inhibited by cyanide (K-i similar to 2.5 mu M) and azide. The activity, possibly associated with heme-b(595), was also observed in catalase-deficient E. coli cells following cytochrome bd over-expression suggesting a protective role against oxidative stress in vivo. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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