Differential calmodulin-modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant

Satya P. Panda, Wenbing Li, Priya Venkatakrishnan, Li Chen, Andrei V. Astashkin, Bettie Sue S. Masters, Changjian Feng, Linda J. Roman

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Neuronal nitric oxide synthase μ (nNOSμ) contains 34 additional residues in an autoregulatory element compared to nNOSα. Cytochrome c and flavin reductions in the absence of calmodulin (CaM) were faster in nNOSμ than nNOSα, while rates in the presence of CaM were smaller. The magnitude of stimulation by CaM is thus notably lower in nNOSμ. No difference in NO production was observed, while electron transfer between the FMN and heme moieties and formation of an inhibitory ferrous-nitrosyl complex were slower in nNOSμ. Thus, the insert affects electron transfer rates, modulation of electron flow by CaM, and heme-nitrosyl complex formation.

Original languageEnglish (US)
Pages (from-to)3973-3978
Number of pages6
JournalFEBS Letters
Volume587
Issue number24
DOIs
StatePublished - Dec 11 2013

Keywords

  • Calmodulin
  • Electron transfer
  • Flavoproteins
  • Heme
  • Neuronal nitric oxide synthase
  • Reductase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Differential calmodulin-modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant'. Together they form a unique fingerprint.

  • Cite this