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首页> 外文期刊>Biochemistry >Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase.
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Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase.

机译：神经元型一氧化氮合酶中电子转移的构象和热力学控制。

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摘要

Multiple solution-state techniques have been employed in investigating the nature and control of electron transfer in the context of the proposed "domain shuffle hypothesis" for intraprotein electron transfer inferred from the crystal structure of the nitric oxide synthase reductase domain. NADPH analogues and fragments have been used to map those regions of this substrate that are important in eliciting a conformational change, observed in both the fluorescence emission of the flavin cofactors of the enzyme and the EPR spectra of the FMN flavosemiquinone state. EPR and UV-visible potentiometric methods have demonstrated a substantial calmodulin-dependent perturbation in the midpoint reduction potentials of the redox couples of both flavin cofactors, in contrast to a previous report [Noble, M. A., et al. (1999) Biochemistry 38, 16413-16418]. These studies support a model in which FMN domain mobility, triggered by Ca2+-calmodulin binding and antagonized by substrate binding, facilitates electron transfer in nitric oxide synthase through conformational change and effects a major change in the midpoint reduction potentials of the flavin redox couples. These results are discussed in light of the recent crystal structure of the NADPH-locked reductase domain.
机译：在从氮氧化物合酶还原酶结构域的晶体结构推断出的蛋白质内电子转移的“域改组假说”的背景下，已采用多种溶液状态技术来研究电子转移的性质和控制。 NADPH类似物和片段已用于绘制该底物在引发构象变化中重要的区域的图，这在该酶的黄素辅因子的荧光发射和FMN黄酮半醌状态的EPR光谱中均观察到。与以前的报道相反，EPR和紫外可见电位法已证明两种黄素辅助因子的氧化还原对的中点还原电位均存在钙调蛋白依赖性的扰动，与先前的报道相反[Noble，M.A。，等。 （1999）Biochemistry 38，16413-16418]。这些研究支持一个模型，在该模型中，由Ca2 +-钙调蛋白结合触发并受底物结合拮抗的FMN域迁移性通过构象变化促进一氧化氮合酶中的电子转移，并影响黄素氧化还原对的中点还原电位的重大变化。鉴于NADPH锁定的还原酶结构域的最新晶体结构，讨论了这些结果。

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