Characterization of endothelial nitric-oxide synthase and its reaction with ligand by electron paramagnetic resonance spectroscopy.

The Journal of Biological Chemistry
A L TsaiG Palmer

Abstract

Electron paramagnetic resonance was used to characterize the heme structure of resting endothelial nitric-oxide synthase (eNOS), eNOS devoid of its myristoylation site (G2A mutant), and their heme complexes formed with 16 different ligands. Resting eNOS and the G2A mutant have a mixture of low spin and high spin P450-heme with widely different relaxation behavior and a stable flavin semiquinone radical identified by EPR as a neutral radical. This flavin radical showed efficient electron spin relaxation as a consequence of dipolar interaction with the heme center; P1/2 is independent of Ca2+-calmodulin and tetrahydrobiopterin. Seven of the 16 ligands led to the formation of low spin heme complexes. In order of increasing rhombicity they are pyrimidine, pyridine, thiazole, L-lysine, cyanide, imidazole, and 4-methylimidazole. These seven low spin eNOS complexes fell in a region between the P and O zones on the "truth diagram" originally derived by Blumberg and Peisach (Blumberg, W. E., and Peisach, J. (1971) in Probes and Structure and Function of Macromolecules and Membranes (Chance, B., Yonetani, T., and Mildvan, A. S., eds) Vol. 2, pp. 215-229, Academic Press, New York) and had significant overlap with complexes of chloroperoxi...Continue Reading

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Citations

Apr 11, 2001·Journal of Inorganic Biochemistry·S Adak, D J Stuehr
Jun 25, 2010·Biochemistry·Ah-Lim TsaiJohn S Olson
Aug 11, 2010·Journal of the American Chemical Society·Andrei V AstashkinChangjian Feng
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Jun 9, 2004·Steroids·Norio KagawaShiro Yoshioka
Jul 14, 2014·Journal of Inorganic Biochemistry·Vladimír BerkaAh-Lim Tsai
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