1H NMR investigation of the solution structure of substrate-free human heme oxygenase: Comparison to the cyanide-inhibited, substrate-bound complex

Journal of Biological Chemistry

Volumn 279, Issue 11, 2004, Pages 10195-10205

  Li, Yiming ^a   Syvitski, Ray T ^a   Auclair, Karine ^b,c   Ortiz De Montellano, Paul R ^b   La Mar, Gerd N ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARAMAGNETISM; PORPHYRINS; WATER;

LIGANDS;

ENZYMES;

CYANIDE; HEME OXYGENASE; ASPARTIC ACID; CARBOXYLIC ACID; LIGAND; PROTON; TYROSINE; WATER;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CATALYSIS; COMPLEX FORMATION; ELECTRON TRANSPORT; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; MEMBRANE BINDING; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RAT; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN CONFORMATION; THERMODYNAMICS;

ANIMALIA;

ASPARTIC ACID; CARBOXYLIC ACIDS; CYANIDES; HEME OXYGENASE (DECYCLIZING); HUMANS; HYDROGEN BONDING; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTONS; THERMODYNAMICS; TYROSINE; WATER;

EID: 1642385047     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M308379200     Document Type: Article

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