Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe-S maturase proteins HydE, HydF, and HydG.
Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe-S maturase proteins HydE, HydF, and HydG.
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DOI：
10.1039/d0sc04216a
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发表时间：
2020-09-22
期刊：
影响因子：
8.4
通讯作者：
Tao L
中科院分区：
文献类型：
--
作者：
Britt RD;Rao G;Tao L
[FeFe]氢酶在一个复杂的Fe-S活性中心进行质子和分子氢(2H++2E−⇌H2)的氧化还原相互转化，称为H-簇。H-簇由一个[4Fe-4S]亚簇组成，这里记为[4Fe]H，通过半胱氨酸硫连接到一个有趣的有机金属[2Fe]H亚簇，被认为是催化发生的亚基。这个[2Fe]H亚簇由两个Fe原子组成，分别与一个桥联的CO和一个桥联的SCH_2NHCH_2S氮二硫酸酯(ADT)相连，每个Fe上都有额外的末端CO和CN配体。合成这样一个复杂的有机金属单元是生物化学中一个令人着迷的问题，因为CO和CN−物种的毒性性质以及氮杂二硫酸酯桥的相对易损性使其变得复杂。多年来，人们已经知道这种复杂的生物合成是由三种必需的铁-S蛋白进行的，即Hyde、HydF和HydG。HydF是一种GTP酶，而Hyde和HydG都是自由基S-腺苷蛋氨酸(RSAM)酶家族的成员。从这个角度，我们描述了这三种铁-S“成熟酶”蛋白的研究和发现的历史，并描述了最近的证据，从rSAM酶HydG合成单核金属有机金属[Fe(II)(CO)2CN(半胱氨酸)]络合物开始，然后被第二个rSAM酶Hyde激活，形成高活性的Fe(I)(CO)2(CN)S物种。在我们的模型中，一对这样的Fe(I)(CO)2(CN)S单元缩合形成[2Fe]H团簇的[Fe(CO)2(CN)S]2钻石核，只需要安装氮二硫醇桥的中心CH2NHCH2部分，其原子都来自氨基酸丝氨酸。这最后一步很可能发生在海德和海德福的相互作用中，细节仍有待阐明。铁-S簇酶HydG、Hyde和HydF提供[FeFe]氢酶催化H-簇的顺序组装。
[FeFe] hydrogenases carry out the redox interconversion of protons and molecular hydrogen (2H+ + 2e− ⇌ H2) at a complex Fe–S active site known as the H-cluster. The H-cluster consists of a [4Fe–4S] subcluster, denoted here as [4Fe]H, linked via a cysteine sulfur to an interesting organometallic [2Fe]H subcluster thought to be the subsite where the catalysis occurs. This [2Fe]H subcluster consists of two Fe atoms, linked with a bridging CO and a bridging SCH2NHCH2S azadithiolate (adt), with additional terminal CO and CN ligands bound to each Fe. Synthesizing such a complex organometallic unit is a fascinating problem in biochemistry, complicated by the toxic nature of both the CO and CN− species and the relative fragility of the azadithiolate bridge. It has been known for a number of years that this complex biosynthesis is carried out by a set of three essential Fe–S proteins, HydE, HydF, and HydG. HydF is a GTPase, while HydE and HydG are both members of the large family of radical S-adenosylmethionine (rSAM) enzymes. In this perspective we describe the history of research and discovery concerning these three Fe–S “maturase” proteins and describe recent evidence for a sequential biosynthetic pathway beginning with the synthesis of a mononuclear organometallic [Fe(ii)(CO)2CN(cysteine)] complex by the rSAM enzyme HydG and its subsequent activation by the second rSAM enzyme HydE to form a highly reactive Fe(i)(CO)2(CN)S species. In our model a pair of these Fe(i)(CO)2(CN)S units condense to form the [Fe(CO)2(CN)S]2 diamond core of the [2Fe]H cluster, requiring only the installation of the central CH2NHCH2 portion of the azadithiolate bridge, whose atoms are all sourced from the amino acid serine. This final step likely occurs with an interplay of HydE and HydF, the details of which yet remain to be elucidated. Fe–S cluster enzymes HydG, HydE, and HydF provide sequential assembly of the catalytic H-cluster of [FeFe] hydrogenase.
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