Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.

Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.
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DOI:
10.1002/1873-3468.13870
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发表时间:
2020-09
期刊:
影响因子:
3.5
通讯作者:
Feng C
Feng C
中科院分区:
生物学3区
文献类型:
--
作者:
Zheng H;Li J;Feng C

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用纯化的二聚体人热休克蛋白90 α(Hsp 90 α)研究Hsp 90 α是否影响一氧化氮合酶(NOS)的一个重要步骤--铁锰血红素结构域间电子传递(IET)。大鼠神经元NOS(nNOS)的IET率显示出显着的增加后,加入热休克蛋白90在剂量饱和的方式,和效果被取消了一个单一的电荷中和突变在保守的热休克蛋白90 K585。添加Ficoll 70的动力学结果进一步表明,Hsp 90通过与nNOS结合影响IET。热休克蛋白90的影响可能是通过缩小FMN结构域运动的可用构象空间。
Purified dimeric human Hsp90α was used to investigate whether Hsp90 affects the FMN–heme interdomain electron transfer (IET), an essential step in nitric oxide synthase (NOS). The IET rate for rat neuronal NOS (nNOS) displayed a noticeable increase upon adding Hsp90 in a dose-saturable manner, and the effect was abolished by a single charge-neutralization mutation at conserved Hsp90 K585. The kinetic results with added Ficoll 70 further suggest that Hsp90 influences the IET through association with nNOS. The Hsp90 effect is presumably via narrowing the available conformational space for the FMN domain motions.
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