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Journal ArticleDOI

Catalase activity of oxygenase domain of rat neuronal nitric oxide synthase. Evidence for product formation from L-arginine.

Sanjay Adhikari, +2 more
- 09 Jun 2000 - 
- Vol. 475, Iss: 1, pp 35-38
TLDR
This work purified the heme containing, tetrahydrobiopterin‐free, oxygenase domain of rat neuronal nitric oxide synthase overexpressed in Escherichia coli and found catalase activity in nNOSox.
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This article is published in FEBS Letters.The article was published on 2000-06-09. It has received 9 citations till now. The article focuses on the topics: Nitric oxide synthase & Nitric oxide.

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Journal ArticleDOI

Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism.

TL;DR: H4B is not essential for Arg oxidation by nNOS, although it helps couple NADPH oxidation to product formation in both steps of NO synthesis, and the NADPH- or H2O2-driven reactions form common heme-oxy species that can react with substrate in the presence or absence of H4B.
Journal ArticleDOI

Bacterial nitric oxide synthases.

TL;DR: Spectroscopic studies of thermostable bacterial NOSs have revealed key oxyheme intermediates involved in the oxidation of substrate L-arginine to product NO, disclosing new roles for NO in biology, such as taking part in toxin biosynthesis, protection against oxidative stress, and regulation of recovery from radiation damage.
Journal ArticleDOI

Tetrahydrobiopterin and nitric oxide: mechanistic and pharmacological aspects.

TL;DR: This review summarizes the current view of how tetrahydrobiopterin functions in the generation of NO and focuses on pharmacological aspects of tetrahytochemical availability with emphasis on endothelial function.
Journal ArticleDOI

First Half-Reaction Mechanism of Nitric Oxide Synthase: The Role of Proton and Oxygen Coupled Electron Transfer in the Reaction by Quantum Mechanics/Molecular Mechanics

TL;DR: The cofactor H(4)B turns out to be a key player in the mechanism acting alternatively as an electron donor and an electron sink and, thereby, providing the electron transfer component in the various coupled proton and oxygen transfer steps.
Journal ArticleDOI

What does "NO-Synthase" stand for ?

TL;DR: In this article, the authors address the relationship between structure, function and evolution of NOS proteins using three NOS model families and advocates for an integrative and interdisciplinary approach that combines modelling studies, structural characterization, and in vitro/in vivo functional investigations.
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