ArticleThe FEBS journal2013
Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.
Article in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Human skeletal muscle nitrate store: influence of dietary nitrate supplementation and exercise.The Journal of physiology · 2019Trial
- Reactions of Recombinant Neuronal Nitric Oxide Synthase with Redox Cycling Xenobiotics: A Mechanistic Study.International journal of molecular sciences · 2022Article
- Mechanism and regulation of ferrous heme-nitric oxide (NO) oxidation in NO synthases.The Journal of biological chemistry · 2019Article
- A docked state conformational dynamics model to explain the ionic strength dependence of FMN - heme electron transfer in nitric oxide synthase.Journal of inorganic biochemistry · 2018Article
- Exploring the conformations of nitric oxide synthase with fluorescence.Frontiers in bioscience (Landmark edition) · 2018Review
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- A perspective on conformational control of electron transfer in nitric oxide synthases.Nitric oxide : biology and chemistry · 2017Review
- The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength.Frontiers in pharmacology · 2017Article
- Signaling and stress: The redox landscape in NOS2 biology.Free radical biology & medicine · 2015Review
- Dissecting structural and electronic effects in inducible nitric oxide synthase.The Biochemical journal · 2015Article
- Energy landscapes and catalysis in nitric-oxide synthase.The Journal of biological chemistry · 2014Article
- Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Journal of inorganic biochemistry · 2014Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
NO synthase (NOS) enzymes convert L-arginine to NO in two sequential reactions whose rates (k(cat1) and k(cat2)) are both limited by the rate of ferric heme reduction (k(r)). An enzyme ferric heme-NO complex forms as an immediate product complex and then undergoes either dissociation (at a rate that we denote as k(d)) to release NO in a productive manner, or reduction (k(r)) to form a ferrous heme-NO complex that must react with O2 (at a rate that we denote as k(ox)) in a NO dioxygenase reaction that regenerates the ferric enzyme. The interplay of these five kinetic parameters (k(cat1), k(cat2), k(r), k(d) and k(ox)) determines NOS specific activity, O2 concentration response, and pulsatile versus steady-state NO generation. In the present study, we utilized stopped-flow spectroscopy and single catalytic turnover methods to characterize the individual temperature dependencies of the five kinetic parameters of rat neuronal NOS. We then incorporated the measured kinetic values into computer simulations of the neuronal NOS reaction using a global kinetic model to comprehensively model its temperature-dependent catalytic behaviours. The results obtained provide new mechanistic insights and also reveal that the different temperature dependencies of the five kinetic parameters significantly alter neuronal NOS catalytic behaviours and NO release efficiency as a function of temperature.
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Registered trials
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