@article{6b2d0031468e4719b9f0a7fa2dfd12ce,
title = "Differential calmodulin-modulatory and electron transfer properties of neuronal nitric oxide synthase mu compared to the alpha variant",
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 = "Calmodulin, Electron transfer, Flavoproteins, Heme, Neuronal nitric oxide synthase, Reductase",
author = "Panda, {Satya P.} and Wenbing Li and Priya Venkatakrishnan and Li Chen and Astashkin, {Andrei V.} and Masters, {Bettie Sue S.} and Changjian Feng and Roman, {Linda J.}",
note = "Funding Information: The authors thank Dr. Kenneth M. Roberts, Dept. of Biochemistry, UTHSCSA , for his help in acquiring some of the stopped-flow data. This work was supported by NIH GM052419 to L.J.R. and B.S.M., NIH GM081811 to C.F., NSF CHE-1150644 to C.F., and AHA Grant-in-Aid 12GRNT11780019 to C.F. This project was also supported by grants from the National Center for Research Resources ( 5P20RR016480-12 ) and the National Institute of General Medical Sciences ( 8 P20 GM103451-12 ). B.S.M. is the Robert A. Welch Distinguished Chair in Chemistry (AQ0012). ",
year = "2013",
month = dec,
day = "11",
doi = "10.1016/j.febslet.2013.10.032",
language = "English (US)",
volume = "587",
pages = "3973--3978",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "24",
}