The Astrobiology Biogeocatalysis Research Center and the Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, United States.
Curr Opin Chem Biol. 2011 Apr;15(2):319-27. doi: 10.1016/j.cbpa.2011.02.012. Epub 2011 Mar 8.
Recent advances in our understanding of the mechanisms for the biosynthesis of the complex iron-sulfur (Fe-S) containing prosthetic groups associated with [FeFe]-hydrogenases and nitrogenases have revealed interesting parallels. The biosynthesis of the H-cluster ([FeFe]-hydrogenase) and the FeMo-co (nitrogenase) occurs through a coordinated process that involves the modification of Fe-S cluster precursors synthesized by the general host cell machinery (Isc/Suf). Key modifications to the Fe-S precursors are introduced by the activity of radical S-adenosylmethionine (SAM) enzymes on unique scaffold proteins. The transfer of the modified clusters to a cofactor-less structural apo-protein completes maturation. Together these features provide the basis for establishing unifying paradigms for complex Fe-S cluster biosynthesis for these enzymes.
近年来，我们对与 [FeFe]-氢化酶和氮酶相关的含复杂铁硫 (Fe-S) 辅因子的生物合成机制的理解取得了一些进展，揭示了有趣的相似之处。[FeFe]-氢化酶的 H 簇和氮酶的 FeMo-co 的生物合成是通过一个协调的过程发生的，该过程涉及到由一般宿主细胞机制（Isc/Suf）合成的 Fe-S 簇前体的修饰。Fe-S 前体的关键修饰是由活性的自由基 S-腺苷甲硫氨酸 (SAM) 酶在独特的支架蛋白上引入的。经过修饰的簇转移到没有辅助因子的结构 apo-蛋白上，完成成熟过程。这些特征为这些酶的复杂 Fe-S 簇生物合成建立统一的范例提供了基础。
