Superoxide generation by endothelial nitric oxide synthase: the influence of cofactors.
- J. Vasquez-Vivar, B. Kalyanaraman, K. Pritchard
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 4 August 1998
Results demonstrate that superoxide is generated from the oxygenase domain by dissociation of the ferrous-dioxygen complex and that occupation of the L-arginine binding site does not inhibit this process, and indicate that modulation of BH4 concentration may regulate the ratio of superoxide to nitric oxide generated by eNOS.
Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.
- M. Wang, D. L. Roberts, R. Paschke, T. Shea, B. Masters, J. J. Kim
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 5 August 1997
The structure of rat liver CPR, expressed in Escherichia coli and solubilized by limited trypsinolysis, has been determined by x-ray crystallography at 2.6 A resolution.
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin
- G. Garcı́a-Cardeña, P. Martásek, W. Sessa
- Biology, ChemistryJournal of Biological Chemistry
- 10 October 1997
The data demonstrate a novel functional role for Caveolin-1 in mammalian cells as a potential molecular chaperone that directly inactivates NOS and the inactivation of eNOS and nNOS by the scaffolding domain of caveolin-3 suggests that eN OS in cardiac myocytes and n NOS in skeletal muscle are likely subject to negative regulation by this muscle-specific caveolin isoform.
Crystal Structure of Constitutive Endothelial Nitric Oxide Synthase A Paradigm for Pterin Function Involving a Novel Metal Center
- C. Raman, Huiying Li, P. Martásek, V. Král, B. Masters, T. Poulos
- Biology, ChemistryCell
- 23 December 1998
Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography.
- Y. Yasukochi, B. Masters
- Biology, ChemistryJournal of Biological Chemistry
- 10 September 1976
Inducible Nitric-oxide Synthase Generates Superoxide from the Reductase Domain*
- Yong Xia, L. Roman, B. Masters, J. Zweier
- Biology, ChemistryJournal of Biological Chemistry
- 28 August 1998
Electron paramagnetic resonance measurements demonstrate that inducible NOS does generate O⨪2, and this mainly occurs at the flavin-binding sites of the reductase domain.
Effects of 17-octadecynoic acid, a suicide-substrate inhibitor of cytochrome P450 fatty acid omega-hydroxylase, on renal function in rats.
The results suggest that endogenous cytochrome P450 metabolites of arachidonic acid influence renal medullary hemodynamics and the excretion of water and electrolytes.
Endothelial nitric oxide synthase-dependent superoxide generation from adriamycin.
- J. Vasquez-Vivar, P. Martásek, N. Hogg, B. Masters, K. Pritchard, B. Kalyanaraman
- Biology, ChemistryBiochemistry
- 23 September 1997
It is demonstrated here that the endothelial isoform of nitric oxide synthase (eNOS) reduces adriamycin to the semiquinone radical, which enhances superoxide formation and Nitric oxide production and leads eNOS to generate peroxynitrite and hydrogen peroxide, potent oxidants implicated in several vascular pathologies.
Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency
- C. Xia, S. Panda, C. Marohnic, P. Martásek, B. Masters, Jung‐Ja P. Kim
- BiologyProceedings of the National Academy of Sciences
- 1 August 2011
CYPOR dysfunction in patients harboring these particular mutations may possibly be prevented by riboflavin therapy in utero, if predicted prenatally, or rescued postnatally in less severe cases.
An Autoinhibitory Control Element Defines Calcium-regulated Isoforms of Nitric Oxide Synthase*
- J. Salerno, Dawn E. Harris, S. Gross
- Biology, ChemistryJournal of Biological Chemistry
- 21 November 1997
It is shown that cNOS isoforms contain a unique polypeptide insert in their FMN binding domains which is not shared with iNOS or other related flavoproteins, and this strongly suggest that the insert is an autoinhibitory control element, docking with a site on cN OSs which impedes calmodulin binding and enzymatic activation.
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