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铁硫黄素酶：使最古老的氧化还原辅因子和多功能黄素协同工作的附加值。

Iron-sulfur flavoenzymes: the added value of making the most ancient redox cofactors and the versatile flavins work together.

机构信息

Dipartimento di Bioscienze, Università degli Studi di Milano, Via Celoria 26, 20133 Milano, Italy.

出版信息

Open Biol. 2021 May;11(5):210010. doi: 10.1098/rsob.210010. Epub 2021 May 5.

DOI:10.1098/rsob.210010
PMID:33947244
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8097209/
Abstract

Iron-sulfur (Fe-S) flavoproteins form a broad and growing class of complex, multi-domain and often multi-subunit proteins coupling the most ancient cofactors (the Fe-S clusters) and the most versatile coenzymes (the flavin coenzymes, FMN and FAD). These enzymes catalyse oxidoreduction reactions usually acting as switches between donors of electron pairs and acceptors of single electrons, and vice versa. Through selected examples, the enzymes' structure-function relationships with respect to rate and directionality of the electron transfer steps, the role of the apoprotein and its dynamics in modulating the electron transfer process will be discussed.

摘要

铁硫（Fe-S）黄素蛋白形成了一个广泛且不断发展的复杂、多结构域且通常多亚基蛋白类群，它们将最古老的辅因子（Fe-S 簇）和最通用的辅酶（黄素辅酶，FMN 和 FAD）结合在一起。这些酶通常作为电子对供体和单电子受体之间的开关，催化氧化还原反应，并可以相互转换。通过选择的实例，将讨论酶的结构-功能关系，包括电子转移步骤的速率和方向性、脱辅基蛋白的作用及其在调节电子转移过程中的动力学。

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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba0f/8097209/6381a55217c7/rsob210010f06.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba0f/8097209/dd28fc6d99e3/rsob210010f07.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba0f/8097209/958ef2efa461/rsob210010f08.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba0f/8097209/7464352a130d/rsob210010f09.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba0f/8097209/ff786993e4db/rsob210010f11.jpg

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