Enzymatic Systems with Homology to Nitrogenase: Biosynthesis of Bacteriochlorophyll and Coenzyme F430.
Enzymatic Systems with Homology to Nitrogenase: Biosynthesis of Bacteriochlorophyll and Coenzyme F430.
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与固氮酶同源的酶系统：细菌叶绿素和辅酶 F430 的生物合成
DOI：
10.1007/978-1-4939-8864-8_2
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发表时间：
2019
影响因子：
--
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与固氮酶同源的酶对于细菌叶绿素和辅酶F430的生物合成途径内的化学稳定双键的还原是必不可少的。这些基于四吡咯的化合物对于细菌光合作用和产甲烷古菌中甲烷的生物发生至关重要。细菌叶绿素的形成需要独特的ATP依赖性酶叶绿素氧化还原酶（COR）的两个电子还原叶绿素细菌叶绿素。COR催化基于同二聚体蛋白质亚基BchX 2，其促进电子转移到相应的异四聚体催化亚基（BchY/BchZ）2。与固氮酶系统类似，动态开关蛋白BchX 2包含一个[4Fe-4S]簇，该簇触发ATP驱动的电子转移到位于（BchY/BchZ）2中的第二个[4Fe-4S]簇上。随后的底物还原和质子化与固氮酶催化无关，没有进一步参与含氘的辅因子。含镍辅酶F430的生物合成包括在CfbC/D催化下Ni 2 +-sirohydrochlorina，c-diamide的四吡咯大环六电子还原为Ni 2 +-hexahydrosirohydrochlorina，c-diamide。携带[4Fe-4S]簇的同源二聚体CfbC 2亚基与BchX 2具有密切的同源性。因此，提出了CfbC/D的初始ATP驱动的电子转移步骤的平行性。电子被二聚催化亚基CfbD 2接收，CfbD 2包含第二个[4Fe-4S]簇，并在高度协调的空间和区域选择性过程中实现三个双键的饱和。在对固氮酶催化进行简短介绍之后，本章将重点介绍了解固氮酶样酶COR和CfbC/D的最新进展，特别强调潜在的酶促机制。
Enzymes with homology to nitrogenase are essential for the reduction of chemically stable double bonds within the biosynthetic pathways of bacteriochlorophyll and coenzyme F430. These tetrapyrrole-based compounds are crucial for bacterial photosynthesis and the biogenesis of methane in methanogenic archaea. Formation of bacteriochlorophyll requires the unique ATP-dependent enzyme chlorophyllide oxidoreductase (COR) for the two-electron reduction of chlorophyllide to bacteriochlorophyllide. COR catalysis is based on the homodimeric protein subunit BchX2, which facilitates the transfer of electrons to the corresponding heterotetrameric catalytic subunit (BchY/BchZ)2. By analogy to the nitrogenase system, the dynamic switch protein BchX2contains a [4Fe-4S] cluster that triggers the ATP-driven transfer of electrons onto a second [4Fe-4S] cluster located in (BchY/BchZ)2. The subsequent substrate reduction and protonation is unrelated to nitrogenase catalysis, with no further involvement of a molybdenum-containing cofactor. The biosynthesis of the nickel-containing coenzyme F430includes the six-electron reduction of the tetrapyrrole macrocycle of Ni2+-sirohydrochlorina,c-diamide to Ni2+-hexahydrosirohydrochlorina,c-diamide catalyzed by CfbC/D. The homodimeric CfbC2subunit carrying a [4Fe-4S] cluster shows close homology to BchX2. Accordingly, parallelism for the initial ATP-driven electron transfer steps of CfbC/D was proposed. Electrons are received by the dimeric catalytic subunit CfbD2, which contains a second [4Fe-4S] cluster and carries out the saturation of an overall of three double bonds in a highly orchestrated spatial and regioselective process. Following a short introduction to nitrogenase catalysis, this chapter will focus on the recent progress toward the understanding of the nitrogenase-like enzymes COR and CfbC/D, with special emphasis on the underlying enzymatic mechanism(s).
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DOI：
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