1H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis: Influence of the axial water deprotonation on the distal H-bond network

Journal of the American Chemical Society

Volumn 128, Issue 20, 2006, Pages 6657-6668

  Ma, Li Hua ^a   Liu, Yangzhong ^a   Zhang, Xuhang ^b   Yoshida, Tadashi ^b   La Mar, Gerd N ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b YAMAGATA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; ELECTRONIC STRUCTURE; HYDROGEN BONDS; MAGNETIC SUSCEPTIBILITY; PARAMAGNETIC MATERIALS; TENSORS;

AXIAL ANISOTROPY; NEISSERIA MENINGITIDIS HEME OXYGENASE (NMHO); PARAMAGNETIC SUSCEPTIBILITY TENSORS; PROTOHEMIN COMPLEX;

ORGANIC COMPOUNDS;

HEME OXYGENASE; HYDROXIDE; HEME; HYDROXIDE ION; WATER;

ANISOTROPY; ARTICLE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HYDROGEN BOND; LIGHT HARVESTING SYSTEM; NEISSERIA MENINGITIDIS; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; RESIDUE ANALYSIS; STRUCTURE ANALYSIS; CHEMISTRY; ENZYMOLOGY; NUCLEAR MAGNETIC RESONANCE; PH; THERMODYNAMICS;

ANISOTROPY; HEME; HEME OXYGENASE (DECYCLIZING); HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROXIDES; NEISSERIA MENINGITIDIS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; THERMODYNAMICS; WATER;

EID: 33646750965     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0584626     Document Type: Article

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