An infrared study of NO bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds.
Biochemistry
; 15(2): 388-96, 1976 Jan 27.
Article
en En
| MEDLINE
| ID: mdl-1247525
Five- and six-coordinate nitrosyl hemes have been prepared and their infrared, electron paramagnetic resonance (EPR), and visible-Soret spectra compared with the corresponding spectra for nitrosyl hemoglobin A (Hba-NO) determined both in the presence and the absence of inositol hexaphosphate (IHP). The five- and six-coordinate NO complexes prepared from either dipyridine or pyridine carbonyl protoheme dimethyl ester had N-O stretch bands (nuno) near 1675 and 1625 cm-1, respectively. These frequencies are sensitive to change in solvent (nuno decreased as the dipole moment of the solvent increased) and, with six-coordinate species, to changes in trans ligand. However, these solvent and trans ligand effects were small compared with the difference (ca. 50 cm-11) between five- and six -coordinate species. The nature of the trans ligand affected the relative proportions of the two...
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ácido Fítico
/
Inositol
/
Óxido Nítrico
Límite:
Humans
Idioma:
En
Revista:
Biochemistry
Año:
1976
Tipo del documento:
Article
Pais de publicación:
Estados Unidos