Peroxidase activity by MnSOD?

Free Radical Biology and Medicine

Volumn 65, Issue , 2013, Pages 1535-

  Liochev, Stefan I ^a   Fridovich, Irwin ^b  

^a Department of Biochemistry Duke University Medical Center ^*  (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Amplex red; Free radicals; Hydrogen peroxide; Resorufin; Signaling; Superoxide; Superoxide dismutase

Indexed keywords

HYDROGEN PEROXIDE; MANGANESE SUPEROXIDE DISMUTASE; OXYGEN; PEROXIDASE;

CATALYSIS; ENZYME ACTIVITY; ENZYME MODIFICATION; LETTER; OXIDATION; PRIORITY JOURNAL; STEADY STATE;

AMPLEX RED; FREE RADICALS; HYDROGEN PEROXIDE; RESORUFIN; SIGNALING; SUPEROXIDE; SUPEROXIDE DISMUTASE;

ANIMALS; HUMANS; MITOCHONDRIA; NEOPLASMS; PEROXIDASE; RECOMBINANT PROTEINS; SUPEROXIDE DISMUTASE;

EID: 84879776298     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.09.034     Document Type: Letter

References (4)

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2. M.B. Yim, P.B. Chock, and E.R. Stadtman Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide Proc. Natl. Acad. Sci. USA 87 1990 5006 5010
3. Ansenberger-Fricano, K.; da Silva Ganini, D.; Mao, M.; Chatterjee, S.; Dallas, S.; Mason, R. P.; Stadler, K.; Santos, J. H.; Bonini, M. G.; The peroxidase activity of mitochondrial superoxide dismutase. Free Radic. Biol. Med., in press, 10.1016/j.freeradbiomed.2012.08.573, URL: 〈 http://www.sciencedirect.com/science/help/doi.htm âŒ
4. B. Zhao, F.A. Summers, and R.P. Mason Photooxidation of Amplex red to resorufin: implications of exposing the Amplex red assay to light Free Radic. Biol. Med. 53 2012 1080 1087