ArticleJournal of inorganic biochemistry2011
Binding kinetics of calmodulin with target peptides of three nitric oxide synthase isozymes.
Article in Journal of inorganic biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Nitric Oxide Signaling in Cardiovascular Physiology and Pathology: Mechanisms, Dysregulation, and Therapeutic Frontiers.International journal of molecular sciences · 2026Review
- Time-resolved solid state NMR of biomolecular processes with millisecond time resolution.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Review
- Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.Journal of the American Chemical Society · 2020Article
- TRPC1 Deficiency Impairs the Endothelial Progenitor Cell Function via Inhibition of Calmodulin/eNOS Pathway.Journal of cardiovascular translational research · 2018Article
- Competitive tuning: Competition's role in setting the frequency-dependence of Ca2+-dependent proteins.PLoS computational biology · 2017Article
- Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encoding.Chemical communications (Cambridge, England) · 2017Article
- A perspective on conformational control of electron transfer in nitric oxide synthases.Nitric oxide : biology and chemistry · 2017Review
- Correlating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic Trap.ACS catalysis · 2016Article
- Molecular architecture of mammalian nitric oxide synthases.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Activation of the Ano1 (TMEM16A) chloride channel by calcium is not mediated by calmodulin.The Journal of general physiology · 2014Article
- Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Journal of inorganic biochemistry · 2014Review
- NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Archives of biochemistry and biophysics · 2012Review
- Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B.Biochemistry · 2012Article
- Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Coordination chemistry reviews · 2012Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Efficient electron transfer from reductase domain to oxygenase domain in nitric oxide synthase (NOS) is dependent on the binding of calmodulin (CaM). Rate constants for the binding of CaM to NOS target peptides was only determined previously by surface plasmon resonance (SPR) (Biochemistry 35, 8742-8747, 1996) suggesting that the binding of CaM to NOSs is slow and does not support the fast electron transfer in NOSs measured in previous and this studies. To resolve this contradiction, the binding rates of holo Alexa 350 labeled T34C/T110W CaM (Alexa-CaM) to target peptides from three NOS isozymes were determined using fluorescence stopped-flow. All three target peptides exhibited fast k(on) constants at 4.5°C: 6.6×10(8)M(-1)s(-1) for nNOS(726-749), 2.9×10(8)M(-1)s(-1) for eNOS(492-511) and 6.1×10(8)M(-1)s(-1) for iNOS(507-531), 3-4 orders of magnitude faster than those determined previously by SPR. Dissociation rates of NOS target peptides from Alexa-CaM/peptide complexes were measured by Ca(2+) chelation with ETDA: 3.7s(-1) for nNOS(726-749), 4.5s(-1) for eNOS(492-511), and 0.063s(-1) for iNOS(507-531). Our data suggest that the binding of CaM to NOS is fast and kinetically competent for efficient electron transfer and is unlikely rate-limiting in NOS catalysis. Only iNOS(507-531) was able to bind apo Alexa-CaM, but in a very different conformation from its binding to holo Alexa-CaM.
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