Emerging concepts in the flavinylation of succinate dehydrogenase.
Emerging concepts in the flavinylation of succinate dehydrogenase.
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DOI：
10.1016/j.bbabio.2013.01.012
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发表时间：
2013-05
影响因子：
4.3
通讯作者：
Winge, Dennis R.
中科院分区：
文献类型：
--
作者：
Kim, Hyung J.;Winge, Dennis R.
琥珀酸脱氢酶(SDH)异四聚体在三羧酸(TCA)循环以及真核生物和细菌的有氧呼吸链中催化琥珀酸氧化成富马酸。在这种催化中必不可少的是SDH酶复合体亚基1(SDH1)中的共价连接辅因子黄素腺嘌呤二核苷酸(FAD)。Fad插入和共价连接到SDH1的机制尚不清楚。我们对这个黄素化过程的工作概念主要依赖于20世纪90年代前的基础工作，并应用了从包含类似链接的FAD的其他酶中学到的原理。然而，黄素化因子Sdh5的发现为与Sdh1黄素化相关的可能机制提供了新的见解，并对与其他黄素酶相关的自催化机制提出了质疑。这篇综述主要集中在了解SDH1的黄素化相关的机制以及这个黄素化过程如何影响SDH的整体组装方面的先前和最近的进展。
The Succinate Dehydrogenase (SDH) heterotetrameric complex catalyzes the oxidation of succinate to fumarate in the tricarboxylic acid (TCA) cycle and in the aerobic respiratory chains of eukaryotes and bacteria. Essential in this catalysis, is the covalently-linked cofactor flavin adenine dinucleotide (FAD) in subunit1 (Sdh1) of the SDH enzyme complex. The mechanism of FAD insertion and covalent attachment to Sdh1 is unknown. Our working concept of this flavinylation process has relied mostly on foundational works from the 1990s ago and by applying the principles learned from other enzymes containing a similarly linked FAD. The discovery of the flavinylation factor Sdh5, however, has provided new insight into the possible mechanism associated with Sdh1 flavinylation, bringing into question the autocatalytic mechanism associated with other flavoenzymes. This review focuses on encapsulating prior and recent advances towards understanding the mechanism associated with flavinylation of Sdh1 and how this flavinylation process affects the overall assembly of SDH.
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影响因子：
4.8
作者：
Bafunno, V;Giancaspero, TA;Barile, M
通讯作者：
Barile, M
DOI：
10.1016/j.ijbiomac.2008.03.001
发表时间：
2008-06-01
影响因子：
8.2
作者：
Brizio, Carmen;Brandsch, Roderich;Barile, Maria
通讯作者：
Barile, Maria
影响因子：
5.4
作者：
Giancaspero, Teresa A.;Locato, Vittoria;Barile, Maria
通讯作者：
Barile, Maria
影响因子：
3.9
作者：
BARILE, M;PASSARELLA, S;QUAGLIARIELLO, E
通讯作者：
QUAGLIARIELLO, E
影响因子：
8.9
作者：
DECKER, KF
通讯作者：
DECKER, KF