NO synthase: Structures and mechanisms

Daff, Simon

doi:10.1016/j.niox.2010.03.001

Cited by 255Nitric Oxide and Endothelin EffectsMetal-Catalyzed Oxygenation MechanismsHemoglobin structure and function

NO synthase: Structures and mechanisms

Daff, Simon·2010·Nitric Oxide

DOI 10.1016/j.niox.2010.03.001

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Abstract

Production of NO from arginine and molecular oxygen is a complex chemical reaction unique to biology. Our understanding of the chemical and regulation mechanisms of the NO synthases has developed over the past two decades, uncovering some extraordinary features. This article reviews recent progress and highlights current issues and controversies. The structure of the enzyme has now been determined almost in entirety, although it is as a selection of fragments, which are difficult to assemble unambiguously. NO synthesis is driven by electron transfer through FAD and FMN cofactors, which is controlled by calmodulin binding in the constitutive mammalian enzymes. Many of the unique structural features involved have been characterised, but the mechanics of calmodulin-dependent activation are largely unresolved. Ultimately, NO is produced in the active site by the reaction of arginine with activated heme-bound oxygen in two distinct cycles. The unique role of the tetrahydrobiopterin cofactor as an electron donor in this process has now been established, but the subsequent chemical events are currently a matter of intense speculation and debate.

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NOS are dimeric, multidomain enzymes that synthesize NO from molecular oxygen and l-arginine and use heme, tetrahydrobiopterin, FAD, FMN, and NADPH as cofactors.
“NOS are dimeric, multidomain enzymes that synthesize NO from molecular oxygen and l-arginine and use iron protoporphyrin-IX (heme), tetrahydrobiopterin (BH4), FAD, flavin mononucleotide (FMN), and NADPH as cofactors”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [204]
The canonical pathways of NO formation rely on the specialized NOS enzymes.
“The canonical pathways of NO formation rely on the specialized NOS enzymes.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [204]
BH4 plays a critical role in the catalytic cycle of NOS.
“In addition, BH4 plays a critical role in the catalytic cycle of NOS (87, 204, 377, 904, 933, 1000, 1007).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [204]

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Catalytic Reduction of a Tetrahydrobiopterin Radical within Nitric-oxide Synthase
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Intraprotein Electron Transfer in a Two-Domain Construct of Neuronal Nitric Oxide Synthase: The Output State in Nitric Oxide Formation
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Electron transfer in human cytochrome P450 reductase
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Removal of a Putative Inhibitory Element Reduces the Calcium-dependent Calmodulin Activation of Neuronal Nitric-oxide Synthase
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The Second Step of the Nitric Oxide Synthase Reaction: Evidence for Ferric-Peroxo as the Active Oxidant
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Characterization of the Roles of the 594–645 Region in Human Endothelial Nitric-oxide Synthase in Regulating Calmodulin Binding and Electron Transfer
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Spectra and Kinetic Studies of the Compound I Derivative of Cytochrome P450 119
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Surface Charge Interactions of the FMN Module Govern Catalysis by Nitric-oxide Synthase
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Single-turnover of Nitric-oxide Synthase in the Presence of 4-Amino-tetrahydrobiopterin
Sørlie, M., Gorren, A. C. F., Marchal, S., Shimizu, T., Lange, R., Andersson, K. K., & Mayer, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305682200 · Cited by 62 · see citing works
A connecting hinge represses the activity of endothelial nitric oxide synthase
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Direct Measurement by Laser Flash Photolysis of Intraprotein Electron Transfer in a Rat Neuronal Nitric Oxide Synthase
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Differential Binding of Calmodulin Domains to Constitutive and Inducible Nitric Oxide Synthase Enzymes
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Effects of Combined Phosphorylation at Ser-617 and Ser-1179 in Endothelial Nitric-oxide Synthase on EC50(Ca2+) Values for Calmodulin Binding and Enzyme Activation
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Redox Function of Tetrahydrobiopterin and Effect of l -Arginine on Oxygen Binding in Endothelial Nitric Oxide Synthase
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The journey from NADPH-cytochrome P450 oxidoreductase to nitric oxide synthases
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Conformational and Thermodynamic Control of Electron Transfer in Neuronal Nitric Oxide Synthase
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Stabilization and Characterization of a Heme-Oxy Reaction Intermediate in Inducible Nitric-oxide Synthase
Tejero, J., Biswas, A., Wang, Z., Page, R. C., Haque, M. M., Hemann, C. F., Zweier, J. L., Misra, S., & Stuehr, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806122200 · Cited by 54 · see citing works
Ability of Tetrahydrobiopterin Analogues to Support Catalysis by Inducible Nitric Oxide Synthase: Formation of a Pterin Radical Is Required for Enzyme Activity
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The FAD-shielding Residue Phe1395 Regulates Neuronal Nitric-oxide Synthase Catalysis by Controlling NADP+ Affinity and a Conformational Equilibrium within the Flavoprotein Domain
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Control of Electron Transfer in Nitric-oxide Synthases
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Differences in a Conformational Equilibrium Distinguish Catalysis by the Endothelial and Neuronal Nitric-oxide Synthase Flavoproteins
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Thermodynamics of Oxidation-Reduction Reactions in Mammalian Nitric-oxide Synthase Isoforms
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Regulation of FMN Subdomain Interactions and Function in Neuronal Nitric Oxide Synthase
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Influence of Myristoylation, Phosphorylation, and Deamidation on the Structural Behavior of the N-Terminus of the Catalytic Subunit of CAMP-Dependent Protein Kinase
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Calmodulin-dependent regulation of mammalian nitric oxide synthase
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A conserved flavin-shielding residue regulates NO synthase electron transfer and nicotinamide coenzyme specificity
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Importance of the Domain−Domain Interface to the Catalytic Action of the NO Synthase Reductase Domain
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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
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Mechanistic Studies on the Intramolecular One-electron Transfer between the Two Flavins in the Human Neuronal Nitric-oxide Synthase and Inducible Nitric-oxide Synthase Flavin Domains
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Structural Analysis of Isoform-Specific Inhibitors Targeting the Tetrahydrobiopterin Binding Site of Human Nitric Oxide Synthases
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Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: Nature and possible function of compound ES☆
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Intraprotein electron transfer in inducible nitric oxide synthase holoenzyme
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The unusual redox properties of flavocytochrome P450 BM3 flavodoxin domain
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Crucial Role of Lys423 in the Electron Transfer of Neuronal Nitric-oxide Synthase
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Self-citation
Versatile Regulation of Neuronal Nitric Oxide Synthase by Specific Regions of Its C-Terminal Tail
Tiso, M., Tejero, J., Panda, K., Aulak, K. S., & Stuehr, D. J. (2007) · Biochemistry · doi:10.1021/bi701646k · Cited by 34 · see citing works
Exploring the Electron Transfer Properties of Neuronal Nitric-oxide Synthase by Reversal of the FMN Redox Potential
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Kinetics of Oxidation of Benzphetamine by Compounds I of Cytochrome P450 2B4 and Its Mutants
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A Density Functional Theory Investigation on the Mechanism of the Second Half-Reaction of Nitric Oxide Synthase
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Deletion of the autoregulatory insert modulates intraprotein electron transfer in rat neuronal nitric oxide synthase
Feng, C., Roman, L. J., Hazzard, J. T., Ghosh, D. K., Tollin, G., & Masters, B. S. S. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.07.005 · Cited by 33 · see citing works
Phosphorylation within an Autoinhibitory Domain in Endothelial Nitric Oxide Synthase Reduces the Ca2+Concentrations Required for Calmodulin To Bind and Activate the Enzyme
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Thermodynamic and Kinetic Analysis of the Nitrosyl, Carbonyl, and Dioxy Heme Complexes of Neuronal Nitric-oxide Synthase
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Self-citation
Redox Properties of the Isolated Flavin Mononucleotide- and Flavin Adenine Dinucleotide-Binding Domains of Neuronal Nitric Oxide Synthase
Garnaud, P. E., Koetsier, M. J., Ost, T. W. B., & Daff, S. N. (2004) · Biochemistry · doi:10.1021/bi049312v · Cited by 30 · see citing works
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The Function of the Small Insertion in the Hinge Subdomain in the Control of Constitutive Mammalian Nitric-oxide Synthases
Jones, R. J., Smith, S. M., Gao, Y. T., DeMay, B. S., Mann, K. J., Salerno, K. M., & Salerno, J. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402808200 · Cited by 27 · see citing works
6-Acetyl-7,7-dimethyl-5,6,7,8-tetrahydropterin is an activator of nitric oxide synthases
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An Appraisal of Multiple NADPH Binding-Site Models Proposed for Cytochrome P450 Reductase, NO Synthase, and Related Diflavin Reductase Systems
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Kinetics and mechanism of the alkaline hydrolysis of guanidine, hexamethylguanidinium perchlorate, and tetramethylurea
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The role of tetrahydrobiopterin in catalysis by nitric oxide synthase
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Davies, S.-A. (2000)

Authors: Daff, S.
Affiliations: University of Edinburgh (GB)
Corresponding author: Daff, Simon
Venue: Nitric Oxide
Publisher: Elsevier BV
Published: 2010-08
Volume: 23
Issue: 1
Pages: 1-11
ISSN: 1089-8603 (ISSN-L)
DOI: 10.1016/j.niox.2010.03.001
OpenAlex: W2030929571
Cited by: 251
References: 135
Citations by year: 2026: 6 · 2025: 5 · 2024: 8 · 2023: 10 · 2022: 10 · 2021: 8 · 2020: 15 · 2019: 14 · 2018: 13 · 2017: 14 · 2016: 23 · 2015: 19 · 2014: 21 · 2013: 27 · 2012: 23
FWCI: 2.82
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Nitric Oxide (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords: nitric oxide synthase, nitric oxide production, enzyme structure, electron transfer, FAD cofactor, FMN cofactor, calmodulin binding, tetrahydrobiopterin, arginine oxidation, enzyme mechanism
MeSH terms: Animals, Humans, Structure-Activity Relationship, Nitric Oxide Synthase

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