Ferric α-hydroxyheme bound to heme oxygenase can be converted to verdoheme by dioxygen in the absence of added reducing equivalents

Journal of Biological Chemistry

Volumn 274, Issue 26, 1999, Pages 18196-18200

  Sakamoto, Hiroshi ^a   Omata, Yoshiaki ^a   Palmer, Graham ^b   Noguchi, Masato ^a  

^a KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b RICE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; FERRIC ION; FERROUS ION; HEME DERIVATIVE; HEME OXYGENASE; OXYGEN; PORPHYRIN DERIVATIVE; POTASSIUM FERRICYANIDE;

ARTICLE; CHEMICAL REACTION; CHEMICAL STRUCTURE; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; HYDROGEN BOND; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MODIFICATION; REACTION ANALYSIS;

ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; FERRIC COMPOUNDS; HEME; HEME OXYGENASE (DECYCLIZING); MODELS, CHEMICAL; OXIDATION-REDUCTION; OXYGEN;

IKEDA;

EID: 0033603348     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.26.18196     Document Type: Article

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