Protonation and hydrogen-bonding state of the distal histidine in the CO complex of horseradish peroxidase as studied by ultraviolet resonance Raman spectroscopy

Biochemistry

Volumn 45, Issue 32, 2006, Pages 9660-9667

  Hashimoto, Shinji ^a   Takeuchi, Hideo ^b  

^a TOKYO UNIVERSITY OF SCIENCE   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON INORGANIC COMPOUNDS; COMPLEXATION; HYDROGEN BONDS; RAMAN SPECTROSCOPY; ULTRAVIOLET RADIATION; WATER;

HISTIDINE (HIS42); HORSERADISH PEROXIDASE (HRP); PROTON DONORS; ULTRAVIOLET RESONANCE RAMAN (UVRR) SPECTROSCOPY;

PROTEINS;

ACID; CARBON MONOXIDE; DEUTERIUM OXIDE; HISTIDINE; HORSERADISH PEROXIDASE; IMIDAZOLE DERIVATIVE; LIGAND; OXIDIZING AGENT;

ARTICLE; CATALYSIS; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROGEN BOND; PH; PKA; PRIORITY JOURNAL; PROTON TRANSPORT; RAMAN SPECTROMETRY; SPECTRUM; ULTRAVIOLET RESONANCE RAMAN SPECTROSCOPY; ULTRAVIOLET SPECTROSCOPY;

BINDING SITES; CARBON MONOXIDE; DEUTERIUM OXIDE; HISTIDINE; HORSERADISH PEROXIDASE; HYDROGEN BONDING; IMIDAZOLES; PROTONS; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN;

ARMORACIA RUSTICANA;

EID: 33747464751     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060466f     Document Type: Article

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