Intra- and inter-molecular effects of a conserved arginine residue of neuronal and inducible nitric oxide synthases on FMN and calmodulin binding

•We mutated the Arg residue of nNOS and iNOS that forms a salt bridge with calmodulin.•Mutation of this Arg in nNOS decreased the calmodulin binding affinity by ∼3-fold.•FMN binding was decreased by 20% for iNOS R530A, 50% for iNOS R530E compared to wild type proteins (WT).•FMN binding was decreased...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2013-05, Vol.533 (1-2), p.88-94
Hauptverfasser:	Panda, Satya Prakash, Polusani, Srikanth R., Kellogg, Dean L., Venkatakrishnan, Priya, Roman, Madeline G., Demeler, Borries, Masters, Bettie Sue S., Roman, Linda J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Arginine calcium Calmodulin Calmodulin - metabolism Cell Line Conserved Sequence crystal structure Electron transfer Electron Transport electrons Flavin Mononucleotide - metabolism Flavoprotein heme humans inducible nitric oxide synthase Kinetics Mice Mutation NADP (coenzyme) neuronal nitric oxide synthase nitric oxide Nitric oxide synthase Nitric Oxide Synthase Type I - chemistry Nitric Oxide Synthase Type I - genetics Nitric Oxide Synthase Type I - isolation & purification Nitric Oxide Synthase Type I - metabolism Nitric Oxide Synthase Type II - chemistry Nitric Oxide Synthase Type II - genetics Nitric Oxide Synthase Type II - isolation & purification Nitric Oxide Synthase Type II - metabolism Protein Binding Rats Reductase Structure-Activity Relationship Ultracentrifugation
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