Characterization of heme-coordinating histidyl residues of cytochrome b5 based on the reactivity with diethylpyrocarbonate: A mechanism for the opening of axial imidazole rings

Journal of Biochemistry

Volumn 140, Issue 4, 2006, Pages 561-571

  Nakanishi, Nobuyuki ^a   Takeuchi, Fusako ^a   Okamoto, Hidetsugu ^a   Tamura, Atsuo ^a   Hori, Hiroshi ^b   Tsubaki, Motonari ^a,c  

^a KOBE UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Cytochrome b5; Diethylpyrocarbonate; Histidyl residue; MALDI TOF; N carbethoxylation

Indexed keywords

CYTOCHROME B5; DIETHYL PYROCARBONATE; HEME; HISTIDINE; IMIDAZOLE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; HYDROGEN BOND; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTON TRANSPORT; RING OPENING; SPECTROSCOPY;

AMINO ACID SEQUENCE; CLONING, MOLECULAR; CYTOCHROMES B5; DIETHYL PYROCARBONATE; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; HISTIDINE; HUMANS; HYDROGEN BONDING; IMIDAZOLES; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 33845343200     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj189     Document Type: Article

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