Oxidation of tryptophan by redox intermediates of myeloperoxidase and inhibition of hypochlorous acid production

Redox Report

Volumn 5, Issue 4, 2000, Pages 179-184

  Kettle, A J ^a   Candaeis, L P ^b  

^a UNIVERSITY OF OTAGO   (New Zealand)

^b MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

HYPOCHLOROUS ACID; MYELOPEROXIDASE; RADICAL; SUPEROXIDE DISMUTASE; TRYPTOPHAN; TYROSINE;

ARTICLE; CATALYSIS; ELECTRON; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; INFLAMMATION; LIPID PEROXIDATION; NEUTROPHIL; OXIDATION; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN CROSS LINKING;

EID: 0033833128     PISSN: 13510002     EISSN: None     Source Type: Journal    
DOI: 10.1179/135100000101535726     Document Type: Article

References (19)

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15. 2.3 A resolution x-ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: A model for a prereaction complex with hydrogen peroxide
16. Superoxide modulates the activity of myeloperoxidase and optimizes the production of hypochlorous acid
17. The diffusion-controlled reaction of semioxidized tryptophan with the superoxide radical anion
18. Nitric oxide rapidly scavenges tyrosine and tryptophan radicals