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Differential calmodulin‐modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant
Author(s) -
Panda Satya P.,
Li Wenbing,
Venkatakrishnan Priya,
Chen Li,
Astashkin Andrei V.,
Masters Bettie Sue S.,
Feng Changjian,
Roman Linda J.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.10.032
Subject(s) - calmodulin , chemistry , heme , nitric oxide synthase , electron transfer , neuronal nitric oxide synthase , atp synthase , nitric oxide , biophysics , stimulation , cytochrome , alpha (finance) , electron transport chain , biochemistry , enzyme , photochemistry , biology , neuroscience , medicine , construct validity , nursing , organic chemistry , patient satisfaction
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.