Differences in Three Kinetic Parameters Underpin the Unique Catalytic Profiles of Nitric-oxide Synthases I, II, and III
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We previously reported the existence of a special auto-regulation property of neuronal nitric-oxide synthase (NOS) based on NO near-geminate combination and partial trapping of neuronal NOS (nNOS) through a futile regenerating pathway. On this basis, we developed a kinetic simulation model that was proven to predict nNOS catalytic specificities and mutations effects (Santolini, J., Adak, S., Curran, C. M., and Stuehr, D. J. (2001) J. Biol. Chem. 276, 1233-1243; Adak, S., Santolini, J., Tikunova, S., Wang, Q., Johnson, J. D., and Stuehr, D. J. (2001) J. Biol. Chem. 276, 1244-1252). Here we show that the same model simulates and explains the distinct catalytic behaviors of inducible and endothelial NOS (iNOS and eNOS). Their marked differences were linked to variations in three basic parameters (rates of ferric heme reduction, ferric heme.NO dissociation, and ferrous heme.NO oxidation) that together control partitioning between futile and productive pathways and their relative rates. We also incorporated feedback inhibition into the kinetic model to account for potential rebinding of accumulated solution NO. The model accurately simulated the different relative impacts of both NOS.NO interactions (near-geminate combination of NO versus rebinding of solution NO) on catalytic behavior of each NOS isoform, including their speed and extent of heme.NO complex accumulation, K(m) for O(2), and propensity to transform NO into a higher oxide. Thus, individual catalytic behavior of any NOS can be understood through a single unified kinetic model. Because the model defines how different settings of individual kinetic parameters control regulation by two distinct NOS.NO interactions, it sheds light on mechanisms, structural features, and scope of NOS regulation and its physiologic impact.
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Tissue from the left ventricle of heart failure patients showed an increase in superoxide production and a decrease in MnSOD protein levels and activity.
“Notably, tissue from the left ventricle of heart failure patients showed an increase in superoxide production and a decrease in MnSOD protein levels and activity, consistent with a role for increased mitochondrial superoxide in the pathogenesis of heart failure (814).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [814]
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A Bridging Interaction Allows Calmodulin to Activate NO Synthase through a Bi-modal Mechanism
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Self-citationActivation of Peroxynitrite by Inducible Nitric-oxide Synthase
Maréchal, A., Mattioli, T. A., Stuehr, D. J., & Santolini, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609237200 · Cited by 37 · see citing works
Self-citationRegulation of the Monomer-Dimer Equilibrium in Inducible Nitric-oxide Synthase by Nitric Oxide
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Endogenous Hemoprotein-Dependent Signaling Pathways of Nitric Oxide and Nitrite
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Self-citationMechanism and regulation of ferrous heme-nitric oxide (NO) oxidation in NO synthases
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Self-citationWhat does ldquo NO-Synthase rdquo stand for
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Fast ferrous heme–NO oxidation in nitric oxide synthases
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A Conserved Aspartate (Asp-1393) Regulates NADPH Reduction of Neuronal Nitric-oxide Synthase
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Self-citationDistinct Influence of N-terminal Elements on Neuronal Nitric-oxide Synthase Structure and Catalysis
Panda, K., Adak, S., Aulak, K. S., Santolini, J., McDonald, J. F., & Stuehr, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304456200 · Cited by 26 · see citing works
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Dynamic Regulation of the Inducible Nitric-oxide Synthase by NO
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Self-citationSpace, time and nitric oxide – neuronal nitric oxide synthase generates signal pulses
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Self-citationInfluence of Heme-Thiolate in Shaping the Catalytic Properties of a Bacterial Nitric-oxide Synthase
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Self-citationCommunication between the Zinc and Tetrahydrobiopterin Binding Sites in Nitric Oxide Synthase
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Self-citationInactivation of nitric oxide by cytochrome c oxidase under steady-state oxygen conditions
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Catalytic Intermediates of Inducible Nitric-oxide Synthase Stabilized by the W188H Mutation*
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Autoinhibition of endothelial nitric oxide synthase (eNOS) in gut smooth muscle by nitric oxide
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Self-citationnNOS uncoupling by oxidized LDL: Implications in atherosclerosis
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NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues
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NO synthase isoforms specifically modify peroxynitrite reactivity
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Nitrate and Nitrite Metabolism in Aging Rats: A Comparative Study
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Engineering nitric oxide synthase chimeras to function as NO dioxygenases
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Self-citation
- Authors
- Santolini, J., Meade, A. L., & Stuehr, D. J.
- Affiliations
- Cleveland Clinic (US)
- Corresponding author
- Stuehr, Dennis J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-12
- Volume
- 276
- Issue
- 52
- Pages
- 48887-48898
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2056420994
- Cited by
- 116
- References
- 68
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 3 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 5 · 2017: 3 · 2016: 3 · 2015: 1 · 2014: 2 · 2013: 7 · 2012: 3
- FWCI
- 4.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- nitric oxide synthase, neuronal nitric oxide synthase, inducible nitric oxide synthase, endothelial nitric oxide synthase, NOS isoforms, autoregulation, product inhibition, nitric oxide metabolism
- MeSH terms
- Heme, Kinetics, Models, Chemical, NADP, Nitric Oxide, Oxidation-Reduction, Nitric Oxide Synthase, Nitric Oxide Synthase Type II, Nitric Oxide Synthase Type I, Nitric Oxide Synthase Type III
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