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J. Biol. Chem., Vol. 268, Issue 30, 22255-22258, Oct, 1993
J Wang, DJ Stuehr, M Ikeda-Saito and DL Rousseau
Nitric oxide (NO), recently found to play many physiological roles, is
generated by the catalysis of L-arginine and O2 to L-citrulline and NO by
nitric oxide synthases (NOSs). Resonance Raman spectra from the heme of
resting, reduced, and CO-bound forms of rat brain NOS firmly establish that
the enzyme belongs to the P-450 class of enzymes. The electron density
marker line (V4) in the Raman spectrum of ligand-free ferrous NOS has a low
frequency (1347 cm-1), indicating a thiolate axial ligand on the heme. The
assignment of a thiolate axial ligand is confirmed in the CO-bound form of
the enzyme by the frequency of the Fe- C-O bending mode at 562 cm-1. The
heme is resting NOS is five- coordinate high spin and thereby differs from
the resting state of most substrate-free P-450s, which are predominantly
six-coordinate low spin. The frequency of the Fe-CO stretching mode in the
CO-bound enzyme at 491 cm-1, identified by isotope substitution, in higher
than that in substrate-free P-450s. Thus, in the ferric and the CO-bound
forms of the enzyme, the sixth-ligand binding site on the heme is
restricted by steric or hydrophobic interactions. In addition, the Fe-CO
stretching mode is broad (30 cm-1) and may be resolved into two overlapping
lines of equal intensity, indicating that the heme domains can adopt two
distinct conformations.
Heme coordination and structure of the catalytic site in nitric oxide synthase
AT&T Bell Laboratories, Murray Hill, New Jersey 07974.
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