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Updated: Jun 23, 2025

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

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对二元化同化NADPH依赖的硫酸盐还原酶的结构揭示了二氨酸还原酶结合的最小接口

Behrouz Ghazi Esfahani1, Nidhi Walia1,2, Kasahun Neselu3

  • 1Department of Biological Science and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL, 32303, USA.

bioRxiv : the preprint server for biology
|June 25, 2024
PubMed
概括

研究人员确定了大肠杆菌硫酸盐还原酶 (SiR) 的第一个近原子分辨率的冷EM结构,揭示了其黄蛋白和血蛋白子单元之间的关键相互作用. 这一突破克服了以前理解SiR的结构性挑战.

关键词:
这是一种NADPH依赖的同化硫酸盐减少酶.低温电磁波冷却器 (Cryo-EM) 是一个非常好的方法.血黄蛋白是血黄蛋白中的一种.氧化减氧剂可以减氧.

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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase10:01

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