The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Spectral characterization of brain and macrophage nitric oxide synthases. Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical.
Open accessAbstract
Nitric oxide (NO) is synthesized in mammals where it acts as a signal molecule for neurotransmission, vasorelaxation, and cytotoxicity. The NO synthases isolated from brain and cytokine-activated macrophages are FAD- and FMN-containing flavoproteins that display considerable sequence homology to NADPH-cytochrome P-450 reductase. However, the nature of their catalytic centers is unknown. We have found that both isoenzymes contain 2 mol of iron-protoporphyrin IX/mol of enzyme homodimer. The optical and EPR spectroscopic properties of the heme groups were found to be remarkably similar to those of high-spin cytochrome P-450. The heme iron in the resting NO synthase is ferric and five-coordinate with a cysteine thiolate as the proximal axial ligand. In addition, the EPR spectra of the resting NO synthases contained a free radical signal attributable to a bound flavin semiquinone that appeared to interact magnetically with the ferric heme iron. NO production was inhibited by carbon monoxide, implying a role for the heme groups in catalysis.
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Cites
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Hemoglobin and myoglobin in their reactions with ligands
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Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
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Cloning and Characterization of Inducible Nitric Oxide Synthase from Mouse Macrophages
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Role of nitric oxide synthesis in macrophage antimicrobial activity
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Cited by
Nitric oxide synthases in mammals
Knowles, R. G., & Moncada, S. (1994) · Biochemical Journal · doi:10.1042/bj2980249 · Cited by 2,752
Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Mammalian nitric oxide synthases
Stuehr, D. J. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00016-x · Cited by 996
Self-citationBaek, K. J., Thiel, B. A., Lucas, S., & Stuehr, D. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36901-7 · Cited by 389
Self-citationModulation of Prostaglandin Biosynthesis by Nitric Oxide and Nitric Oxide Donors
Mollace, V., Muscoli, C., Masini, E., Cuzzocrea, S., & Salvemini, D. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.2.1 · Cited by 357
Metadata
- Authors
- Stuehr, D. J., & Ikeda-Saito, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-10
- Volume
- 267
- Issue
- 29
- Pages
- 20547-20550
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1487443561
- Cited by
- 347
- References
- 45
- FWCI
- 30.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Stuehr, D. J., & Ikeda-Saito, M. (1992). Spectral characterization of brain and macrophage nitric oxide synthases. Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)36718-3
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