Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: Pertinence for determining magnetic axes in paramagnetic substrate complexes

Journal of Inorganic Biochemistry

Volumn 104, Issue 10, 2010, Pages 1063-1070

  Du, Zhenming ^a   Unno, Masaki ^b   Matsui, Toshitaka ^b   Ikeda Saito, Masao ^b   La Mar, Gerd N ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b TOHOKU UNIVERSITY   (Japan)

Author keywords

Aromatic cluster; Corynebacterium diphtheriae; Heme oxygenase; Magnetic axes; Molecular structure

Indexed keywords

CYANIDE; HEME OXYGENASE; BACTERIAL PROTEIN; HEME; HMUO PROTEIN, BACTERIA; PROTON;

ARTICLE; CORYNEBACTERIUM DIPHTHERIAE; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; HUMAN; KINETICS; METABOLISM; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLUTION AND SOLUBILITY;

BACTERIA (MICROORGANISMS); CORYNEBACTERIUM DIPHTHERIAE;

BACTERIAL PROTEINS; CATALYSIS; CORYNEBACTERIUM DIPHTHERIAE; CYANIDES; ENZYME STABILITY; HEME; HEME OXYGENASE (DECYCLIZING); HUMANS; HYDROGEN BONDING; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR STRUCTURE; PROTONS; SOLUTIONS; SUBSTRATE SPECIFICITY;

EID: 77955659803     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2010.06.003     Document Type: Article

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