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Titolo:
X-ray absorption spectroscopic analysis of the high-spin ferriheme site insubstrate-bound neuronal nitric-oxide synthase
Autore:
Cosper, NJ; Scott, RA; Hori, H; Nishino, T; Iwasaki, T;
Indirizzi:
Univ Georgia, Dept Chem, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Georgia, Dept Chem, Athens, GA 30602 USA Nippon Med Coll, Dept Biochem & Mol Biol, Bunkyo Ku, Tokyo 1138602, Japan Nippon Med Coll Tokyo Japan 1138602 iol, Bunkyo Ku, Tokyo 1138602, Japan
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 130, anno: 2001,
pagine: 191 - 198
SICI:
0021-924X(200108)130:2<191:XASAOT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
HYDROXY-L-ARGININE; SCATTERING XAFS ANALYSES; LIGAND BOND LENGTHS; ESCHERICHIA-COLI; CYTOCHROME P-450-CAM; OXYGENASE DIMER; PROXIMAL LIGAND; HEME ENZYMES; NO SYNTHASE; FE-N;
Keywords:
electron paramagnetic resonance spectroscopy; heme; neuronal nitric oxide synthase; nitric oxide synthase; X-ray absorption spectroscopy;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
70
Recensione:
Indirizzi per estratti:
Indirizzo: Iwasaki, T Univ Georgia, Dept Chem, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 pt Chem, Athens, GA 30602 USA
Citazione:
N.J. Cosper et al., "X-ray absorption spectroscopic analysis of the high-spin ferriheme site insubstrate-bound neuronal nitric-oxide synthase", J BIOCHEM, 130(2), 2001, pp. 191-198

Abstract

Nitric oxide synthase (NOS) catalyzes the conversion of L-arginine to citrulline and nitric oxide through two stepwise oxygenation reactions involving N-omega-hydroxy-L-arginine, an enzyme-bound intermediate. The N-omega-hydroxy-L-arginine- and arginine-bound NOS ferriheme centers show distinct, high-spin electron paramagnetic resonance signals. Iron X-ray absorption spectroscopy (XAS) has been used to examine the structure of the ferriheme sitein the N-omega-hydroxy-L-arginine-bound full-length neuronal NOS in the presence of (6R)-5,6,7,8-tetrahydro-L-biopterin. Iron XAS shows that the high-spin ferriheme sites in the N-omega-hydroxy-L-arginine- and arginine-boundforms are strikingly similar, both being coordinated by the heme and an axial thiolate ligand, with an Fe-S distance of ca. 2.29 Angstrom. Cu2+ inhibition slightly affects the spin-state equilibrium, but causes no XAS-detectable changes in the immediate ferriheme coordination environment of neuronal NOS. The structure and ligand geometry of the high-spin ferriheme in arginine-bound neuronal NOS are essentially identical to those of the N-omega-hydroxy-L-arginine-bound form and only slightly affected by the divalent cation inhibitor of consitutive NOS.

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Documento generato il 01/12/20 alle ore 01:12:23