呼吸复合体 I 中的醌化学反应涉及一个保守的天冬氨酸残基的质子化作用

IF 3.5 4区 生物学 Q1 Biochemistry, Genetics and Molecular Biology
Caroline Harter, Frédéric Melin, Franziska Hoeser, Petra Hellwig, Daniel Wohlwend, Thorsten Friedrich
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引用次数: 0

摘要

呼吸复合体 I 是一种将 NADH 氧化和醌还原与质子转运耦合在一起的核心代谢酶。尽管我们已经知道该复合体的结构,但对这两个过程的耦合还不完全了解。在这里,我们结合使用了定点诱变、生化测定和氧化还原诱导傅立叶变换红外光谱法,证明醌的化学作用包括醌结合位点(大肠杆菌 NuoCD 亚基上的 D325)中一个特定的、保守的天冬氨酸残基的质子化和去质子化。我们的实验数据支持从理论上得出的建议,即该残基的去质子化参与触发呼吸复合体 I 中质子的易位。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Quinone chemistry in respiratory complex I involves protonation of a conserved aspartic acid residue
Respiratory complex I is a central metabolic enzyme coupling NADH oxidation and quinone reduction with proton translocation. Despite the knowledge of the structure of the complex, the coupling of both processes is not entirely understood. Here, we use a combination of site‐directed mutagenesis, biochemical assays, and redox‐induced FTIR spectroscopy to demonstrate that the quinone chemistry includes the protonation and deprotonation of a specific, conserved aspartic acid residue in the quinone binding site (D325 on subunit NuoCD in Escherichia coli). Our experimental data support a proposal derived from theoretical considerations that deprotonation of this residue is involved in triggering proton translocation in respiratory complex I.
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来源期刊
FEBS Letters
FEBS Letters 生物-生化与分子生物学
CiteScore
7.00
自引率
2.90%
发文量
303
审稿时长
1.0 months
期刊介绍: FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.
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