No-induced activation mechanism of the heme-regulated eiF2α kinase

Journal of the American Chemical Society

Volumn 124, Issue 46, 2002, Pages 13696-13697

  Ishikawa, Haruto ^a   Yun, Bo Geon ^c   Takahashi, Satoshi ^a   Hori, Hiroshi ^b   Matts, Robert L ^c   Ishimori, Koichiro ^a   Morishima, Isao ^a  

^a KYOTO UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c OKLAHOMA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EIF2ALPHA KINASE; HEME; INITIATION FACTOR 2; NITRIC OXIDE; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CHEMICAL BOND; COMPETITIVE INHIBITION; ELECTRON SPIN RESONANCE; ENZYME ACTIVATION; ENZYME MECHANISM; ENZYME REGULATION; LIGAND BINDING; RAMAN SPECTROMETRY;

CARBON MONOXIDE; EIF-2 KINASE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME ACTIVATION; HEME; HISTIDINE; NITRIC OXIDE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SPECTRUM ANALYSIS, RAMAN;

EID: 0037145993     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0272336     Document Type: Article

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23. We tried to detect the resonance Raman bands of v(FeN-O) and v(Fe-NO) for the ferrous-NO NT-HBD, but ligated NO is photolabile, and the NO-dissociated ferrous NT-HBD was rapidly oxidized. The spectrum after the measurement showed a mixture of the ferrous and ferric forms. Measurements of the infrared spectrum of the ferrous-NO NTHBD have not yet been successful due to the instability of the protein at high concentration.