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

FEBS Lett. 2013 Dec 11;587(24):3973-8. doi: 10.1016/j.febslet.2013.10.032. Epub 2013 Nov 6.

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.

Keywords: AR; C-terminal tail region; CT; CaM; Calmodulin; Electron transfer; Flavoproteins; H(4)B; Heme; IET; NO; NOS; Neuronal nitric oxide synthase; Reductase; autoregulatory region; calmodulin; interdomain electron transfer; l-Arg; l-arginine; nNOS; neuronal NOS; nitric oxide; nitric oxide synthase; tetrahydrobiopterin.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence / physiology
  • Animals
  • Calmodulin / chemistry
  • Calmodulin / metabolism*
  • Cytochromes c / metabolism
  • Electron Transport / physiology
  • Flavin Mononucleotide / metabolism
  • Heme / chemistry
  • Heme / metabolism
  • Isoenzymes / chemistry
  • Isoenzymes / physiology
  • Nitric Oxide / biosynthesis
  • Nitric Oxide Synthase Type I / chemistry
  • Nitric Oxide Synthase Type I / physiology*
  • Protein Binding
  • Rats

Substances

  • Calmodulin
  • Isoenzymes
  • Nitric Oxide
  • Heme
  • Flavin Mononucleotide
  • Cytochromes c
  • Nitric Oxide Synthase Type I