Expression and characterization of full-length human heme oxygenase-1: The presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase

Biochemistry

Volumn 46, Issue 43, 2007, Pages 12212-12219

  Huber III, Warren J ^a   Backes, Wayne L ^a  

^a LOUISIANA STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CARBON MONOXIDE; CATALYSIS; CATALYST ACTIVITY; DEGRADATION; PROTEINS;

ENDOPLASMIC RETICULUM; HUMAN HEME OXYGENASE; LYSINE; OXIDATIVE DEGRADATION;

ENZYME ACTIVITY;

AMINO ACID; ARGININE; BILIRUBIN; BILIVERDIN; CARBON MONOXIDE; FLAVOPROTEIN; GLUTATHIONE TRANSFERASE; HEME; HEME OXYGENASE 1; IRON; LYSINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; THROMBIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME PURIFICATION; GENE MUTATION; MEMBRANE BINDING; OXIDATION; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION;

BASE SEQUENCE; CELL MEMBRANE; DNA PRIMERS; GLUTATHIONE TRANSFERASE; HEME OXYGENASE (DECYCLIZING); HUMANS; NADPH-FERRIHEMOPROTEIN REDUCTASE; PROTEIN BINDING; RECOMBINANT FUSION PROTEINS;

EID: 35648992389     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701496z     Document Type: Article

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