Interaction between inducible nitric oxide synthase and calmodulin in Ca2+-free and -bound forms.

Abstract:

:We have obtained the first direct electrochemistry of full-length inducible nitric oxide synthase (iNOS) by entrapping the enzyme in polyethylenimine (PEI) film. The interaction between iNOS and calmodulin (CaM) was then studied, which revealed an enhanced electron-transfer reactivity of the enzyme facilitated by CaM. It was also found that interflavin electron transfer of iNOS could be activated by the binding of Ca2+-bound CaM. The formal potentials (E degrees ') of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) were determined to be -470 and -284 mV vs SCE at pH 7, respectively. The effect of Ca2+ on the interaction between iNOS and CaM has been examined as well. CaM bound with adequate Ca2+ was shown to have a better capability to enhance the electron-transfer reactions within iNOS.

journal_name

J Proteome Res

authors

Xiao H,Zhou H,Chen G,Liu S,Li G

doi

10.1021/pr060544l

subject

Has Abstract

pub_date

2007-04-01 00:00:00

pages

1426-9

issue

4

eissn

1535-3893

issn

1535-3907

journal_volume

6

pub_type

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