Differential calmodulin-modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant |
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Authors: | Satya P. Panda Wenbing Li Priya Venkatakrishnan Li Chen Andrei V. Astashkin Bettie Sue S. Masters Changjian Feng Linda J. Roman |
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Affiliation: | 1. Department of Biochemistry, University of Texas Health Science Center in San Antonio, San Antonio, TX 78229, USA;2. Department of Pharmaceutical Sciences, College of Pharmacy, University of New Mexico, Albuquerque, NM 87131, USA;3. Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA |
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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. |
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Keywords: | NO, nitric oxide NOS, nitric oxide synthase nNOS, neuronal NOS CaM, calmodulin IET, interdomain electron transfer l-Arg, l-arginine H4B, tetrahydrobiopterin AR, autoregulatory region CT, C-terminal tail region |
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