The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Structure of Nitric Oxide Synthase Oxygenase Dimer with Pterin and Substrate
Abstract
Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate l -arginine ( l -Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and l -Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitric oxide. Pterin binding refolds the central interface region, recruits new structural elements, creates a 30 angstrom deep active-center channel, and causes a 35° helical tilt to expose a heme edge and the adjacent residue tryptophan-366 for likely reductase domain interactions and caveolin inhibition. Heme propionate interactions with pterin and l -Arg suggest that pterin has electronic influences on heme-bound oxygen. l -Arginine binds to glutamic acid–371 and stacks with heme in an otherwise hydrophobic pocket to aid activation of heme-bound oxygen by direct proton donation and thereby differentiate the two chemical steps of nitric oxide synthesis.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,965
The L-Arginine-Nitric Oxide Pathway
Epstein, F. H., Moncada, S., & Higgs, A. (1993) · New England Journal of Medicine · doi:10.1056/nejm199312303292706 · Cited by 6,678
Solvent-Accessible Surfaces of Proteins and Nucleic Acids
Connolly, M. L. (1983) · Science · doi:10.1126/science.6879170 · Cited by 2,745
Sono, M., Roach, M. P., Coulter, E. D., & Dawson, J. H. (1996) · Chemical Reviews · doi:10.1021/cr9500500 · Cited by 2,441
Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
Bredt, D. S., Hwang, P. M., Glatt, C. E., Lowenstein, C., Reed, R. R., & Snyder, S. H. (1991) · Nature · doi:10.1038/351714a0 · Cited by 2,354
Crystallographic R Factor Refinement by Molecular Dynamics
Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,956
Schmidt, H. H. H. W., & Walter, U. (1994) · Cell · doi:10.1016/0092-8674(94)90267-4 · Cited by 1,476
Nitric oxide synthase structure and mechanism
Marletta, M. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31375-9 · Cited by 1,338
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Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110
Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Nitric oxide donors: chemical activities and biological applications
Wang, P. G., Xian, M., Tang, X., Wu, X., Wen, Z., Cai, T., & Janczuk, A. J. (2002) · Chemical Reviews · doi:10.1021/cr000040l · Cited by 1,337
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-citation
Metadata
- Authors
- Crane, B. R., Arvai, A. S., Ghosh, D. K., Wu, C., Getzoff, E. D., Stuehr, D. J., & Tainer, J. A.
- Venue
- Science
- Published
- 1998-03-27
- Volume
- 279
- Issue
- 5359
- Pages
- 2121-2126
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2045639174
- Cited by
- 668
- References
- 35
- FWCI
- 49.93
- Type
- journal article
- Language
- en
- Open access
- closed
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- Crane, B. R., Arvai, A. S., Ghosh, D. K., Wu, C., Getzoff, E. D., Stuehr, D. J., & Tainer, J. A. (1998). Structure of Nitric Oxide Synthase Oxygenase Dimer with Pterin and Substrate. Science. https://doi.org/10.1126/science.279.5359.2121
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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