Výsledky vyhledávání - "B S, Masters"

Akademický článek

Hydrothermal liquefaction: exploring feedstock for sustainable biofuel production.

Autor: Mansuri, Sahir Q.¹, Shekhawat, V. P. S.¹ shekhawatvps@gmail.com

Publikováno v: Environmental & Experimental Biology. 2024, Vol. 22 Issue 3, p135-147. 13p.

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[Nitric oxide synthase, typical flavohemoproteins and their complicated enzymology]

Autor: M, Jáchymová, B S, Masters, K, Horký, T, Zima, P, Martásek

Publikováno v: Casopis lekaru ceskych. 145(7)

Nitric oxide is a diatomic gaseous molecule with unpaired electron in the molecule. Physical properties such as solubility, diffusibility and half-life decide the chemical reactivity of nitric oxide. Nitric oxide is the unstable free radical in vesse

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::acd95e15df4cc3558164b46c255ebdbc
https://pubmed.ncbi.nlm.nih.gov/16921779

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The stimulatory effects of Hofmeister ions on the activities of neuronal nitric-oxide synthase. Apparent substrate inhibition by l-arginine is overcome in the presence of protein-destabilizing agents

Autor: J S, Nishimura, R, Narayanasami, R T, Miller, L J, Roman, S, Panda, B S, Masters

Publikováno v: The Journal of biological chemistry. 274(9)

A variety of monovalent anions and cations were effective in stimulating both calcium ion/calmodulin (Ca2+/CaM)-independent NADPH-cytochrome c reductase activity of, and Ca2+/CaM-dependent nitric oxide (NO.) synthesis by, neuronal nitric oxide syntha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0d458fe80b0d10adb32e317d4e6900ef
https://pubmed.ncbi.nlm.nih.gov/10026150

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Electron spin resonance spin-trapping detection of superoxide generated by neuronal nitric oxide synthase

Autor: J, Vásquez-Vivar, P, Martásek, N, Hogg, H, Karoui, B S, Masters, K A, Pritchard, B, Kalyanaraman

Publikováno v: Methods in enzymology. 301

NOS is a ubiquitous enzyme that has an oxygenase and reductase activity. NOS reduces electron acceptors, at the reductase domain, by a one-electron mechanism that is not inhibited by SOD. One example of this activity is the direct reduction of ferric

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::742edc805e16fc7e2b97e4e0c896d527
https://pubmed.ncbi.nlm.nih.gov/9919565

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Assay of isoforms of Escherichia coli-expressed nitric oxide synthase

Autor: P, Martásek, R T, Miller, L J, Roman, T, Shea, B S, Masters

Publikováno v: Methods in enzymology. 301

The techniques described herein have added to our repertoire of experimental approaches for the characterization of the NOSs. These procedures have reinforced our conviction that the NOSs are structurally suited to perform unique functions in their c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dc3bc8d3d1eb201a13fe5cb8b3d09b8b
https://pubmed.ncbi.nlm.nih.gov/9919555

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Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the nos caveolin binding domain in vivo

Autor: G, García-Cardeña, P, Martasek, B S, Masters, P M, Skidd, J, Couet, S, Li, M P, Lisanti, W C, Sessa

Publikováno v: The Journal of biological chemistry. 272(41)

Endothelial nitric oxide synthase (eNOS) is a dually acylated peripheral membrane protein that targets to the Golgi region and caveolae of endothelial cells. Recent evidence has shown that eNOS can co-precipitate with caveolin-1, the resident coat pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7b0ab04f8701c5ac7a6dd5ab71e1f3f6
https://pubmed.ncbi.nlm.nih.gov/9325253

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Substrate binding-induced changes in the EPR spectra of the ferrous nitric oxide complexes of neuronal nitric oxide synthase

Autor: C T, Migita, J C, Salerno, B S, Masters, P, Martasek, K, McMillan, M, Ikeda-Saito

Publikováno v: Biochemistry. 36(36)

A versatile diatomic physiological messenger, nitric oxide (NO), is biosynthesized by a group of flavo-heme enzymes, the nitric oxide synthases. We have examined the active site of the neuronal isoform by EPR spectroscopy of the ferrous nitric oxide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d61099a88814972dd2362619b2809352
https://pubmed.ncbi.nlm.nih.gov/9283090

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