Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding

Journal of Biological Chemistry

Volumn 282, Issue 29, 2007, Pages 21056-21067

  Yi, Li ^a   Ragsdale, Stephen W ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; CATALYSIS; CELLS; DIFFERENTIAL SCANNING CALORIMETRY; MUTAGENESIS; POTASSIUM; REDOX REACTIONS;

DISULFIDE BONDS; FERRIC HEME; HEME REGULATORY MOTIFS; HOMEOSTASIS; MUTATIONS;

ENZYMES;

CALCIUM ACTIVATED POTASSIUM CHANNEL; CARBON MONOXIDE; CYSTEINE; DISULFIDE; HEME; HEME OXYGENASE 2; THIOL;

ARTICLE; CALORIMETRY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; DISULFIDE BOND; ELECTRON SPIN RESONANCE; ENZYME METABOLISM; HOMEOSTASIS; MUTATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN MOTIF; REDUCTION; REGULATORY MECHANISM; ULTRAVIOLET SPECTROSCOPY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CAROTID BODY; DISULFIDES; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; HEME OXYGENASE (DECYCLIZING); HUMANS; KINETICS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; SULFHYDRYL COMPOUNDS;

EID: 34547121697     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M700664200     Document Type: Article

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