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亚硫酸盐氧化酶

Sulfite oxidizing enzymes.

作者信息

Feng Changjian, Tollin Gordon, Enemark John H

机构信息

College of Pharmacy, University of New Mexico, Albuquerque, NM 87131, USA.

出版信息

Biochim Biophys Acta. 2007 May;1774(5):527-39. doi: 10.1016/j.bbapap.2007.03.006. Epub 2007 Mar 20.

Abstract

Sulfite oxidizing enzymes are essential mononuclear molybdenum (Mo) proteins involved in sulfur metabolism of animals, plants and bacteria. There are three such enzymes presently known: (1) sulfite oxidase (SO) in animals, (2) SO in plants, and (3) sulfite dehydrogenase (SDH) in bacteria. X-ray crystal structures of enzymes from all three sources (chicken SO, Arabidopsis thaliana SO, and Starkeya novella SDH) show nearly identical square pyramidal coordination around the Mo atom, even though the overall structures of the proteins and the presence of additional cofactors vary. This structural information provides a molecular basis for studying the role of specific amino acids in catalysis. Animal SO catalyzes the final step in the degradation of sulfur-containing amino acids and is critical in detoxifying excess sulfite. Human SO deficiency is a fatal genetic disorder that leads to early death, and impaired SO activity is implicated in sulfite neurotoxicity. Animal SO and bacterial SDH contain both Mo and heme domains, whereas plant SO only has the Mo domain. Intraprotein electron transfer (IET) between the Mo and Fe centers in animal SO and bacterial SDH is a key step in the catalysis, which can be studied by laser flash photolysis in the presence of deazariboflavin. IET studies on animal SO and bacterial SDH clearly demonstrate the similarities and differences between these two types of sulfite oxidizing enzymes. Conformational change is involved in the IET of animal SO, in which electrostatic interactions may play a major role in guiding the docking of the heme domain to the Mo domain prior to electron transfer. In contrast, IET measurements for SDH demonstrate that IET occurs directly through the protein medium, which is distinctly different from that in animal SO. Point mutations in human SO can result in significantly impaired IET or no IET, thus rationalizing their fatal effects. The recent developments in our understanding of sulfite oxidizing enzyme mechanisms that are driven by a combination of molecular biology, rapid kinetics, pulsed electron paramagnetic resonance (EPR), and computational techniques are the subject of this review.

摘要

亚硫酸盐氧化酶是参与动物、植物和细菌硫代谢的必需单核钼(Mo)蛋白。目前已知有三种这样的酶:(1)动物体内的亚硫酸盐氧化酶(SO),(2)植物体内的SO,以及(3)细菌体内的亚硫酸盐脱氢酶(SDH)。来自所有这三种来源的酶(鸡SO、拟南芥SO和新金色链霉菌SDH)的X射线晶体结构显示,尽管蛋白质的整体结构和其他辅因子的存在有所不同,但围绕钼原子的配位几乎都是相同的方形金字塔结构。这一结构信息为研究特定氨基酸在催化作用中的作用提供了分子基础。动物SO催化含硫氨基酸降解的最后一步,对过量亚硫酸盐的解毒至关重要。人类SO缺乏是一种致命的遗传疾病,会导致早亡,而SO活性受损与亚硫酸盐神经毒性有关。动物SO和细菌SDH都含有钼和血红素结构域,而植物SO只含有钼结构域。动物SO和细菌SDH中钼和铁中心之间的蛋白质内电子转移(IET)是催化作用中的关键步骤,这可以在脱氮核黄素存在的情况下通过激光闪光光解来研究。对动物SO和细菌SDH的IET研究清楚地证明了这两种亚硫酸盐氧化酶之间的异同。构象变化参与了动物SO的IET,其中静电相互作用可能在电子转移之前引导血红素结构域与钼结构域对接中起主要作用。相比之下,SDH的IET测量表明IET直接通过蛋白质介质发生,这与动物SO明显不同。人类SO中的点突变可导致IET显著受损或无IET,从而解释了它们致命的影响。本文综述了由分子生物学、快速动力学、脉冲电子顺磁共振(EPR)和计算技术相结合推动的我们对亚硫酸盐氧化酶机制理解的最新进展。

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