Interaction between Inducible Nitric Oxide Synthase and Calmodulin in Ca2+-Free and -Bound Forms
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- 作者：Han Xiao ; Hui Zhou ; Guifang Chen ; Shanli Liu ; Genxi Li
- 刊名：Journal of Proteome Research
- 出版年：2007
- 出版时间：April 2007
- 年：2007
- 卷：6
- 期：4
- 页码：1426 - 1429
- 全文大小：124K
- 年卷期：v.6,no.4(April 2007)
- ISSN：1535-3907
文摘
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 facilitatedby CaM. It was also found that interflavin electron transfer of iNOS could be activated by the bindingof Ca2+-bound CaM. The formal potentials (E
') of flavin adenine dinucleotide (FAD) and flavinmononucleotide (FMN) were determined to be -470 and -284 mV vs SCE at pH 7, respectively. Theeffect of Ca2+ on the interaction between iNOS and CaM has been examined as well. CaM bound withadequate Ca2+ was shown to have a better capability to enhance the electron-transfer reactions withiniNOS.
') of flavin adenine dinucleotide (FAD) and flavinmononucleotide (FMN) were determined to be -470 and -284 mV vs SCE at pH 7, respectively. Theeffect of Ca2+ on the interaction between iNOS and CaM has been examined as well. CaM bound withadequate Ca2+ was shown to have a better capability to enhance the electron-transfer reactions withiniNOS.