Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron-Electron Double Resonance Spectroscopy Study.

Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron-Electron Double Resonance Spectroscopy Study.
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氧化还原伴侣连接的亚硝酸铜还原酶的溶液状态铜间分布:脉冲电子-电子双共振光谱研究。

DOI:
10.1021/acs.jpclett.2c01584
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发表时间:
2022-08-04
影响因子:
5.7
通讯作者:
Scrutton, Nigel S.
Scrutton, Nigel S.
中科院分区:
化学2区
文献类型:
--
作者:
Hedison, Tobias M.;Iorgu, Andreea I.;Calabrese, Donato;Heyes, Derren J.;Shanmugam, Muralidharan;Scrutton, Nigel S.

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亚硝酸铜还原酶(CuNiRs)催化亚硝酸盐还原生成一氧化氮。近年来,新的氧化还原伙伴连接的CuNiRs被分离出来,并用结晶学技术进行了表征。溶液状态生物物理研究揭示了这些酶的复杂催化机制,并暗示蛋白质动力学可能在CuNiR催化中发挥作用。为了研究这些CuNiRs的结构、动力学和功能关系,我们使用了蛋白质反向工程和脉冲电子-电子双共振(PELDOR)光谱来确定它们的溶液态铜之间的分布。数据显示了这个酶家族的多维构象图景以及系链在催化中的作用。我们的方法强调了结合高分辨率结晶学技术和低分辨率溶液状态方法来确定金属酶的结构和机制的重要性。
Copper nitrite reductases (CuNiRs) catalyze the reduction of nitrite to form nitric oxide. In recent years, new classes of redox partner linked CuNiRs have been isolated and characterized by crystallographic techniques. Solution-state biophysical studies have shed light on the complex catalytic mechanisms of these enzymes and implied that protein dynamics may play a role in CuNiR catalysis. To investigate the structural, dynamical, and functional relationship of these CuNiRs, we have used protein reverse engineering and pulsed electron–electron double resonance (PELDOR) spectroscopy to determine their solution-state inter-copper distributions. Data show the multidimensional conformational landscape of this family of enzymes and the role of tethering in catalysis. The importance of combining high-resolution crystallographic techniques and low-resolution solution-state approaches in determining the structures and mechanisms of metalloenzymes is emphasized by our approach.
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