Department of Biophysics, Medical College of Wisconsin, 8701 Watertown Plank Rd, Milwaukee, WI, USA, 53226.
Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195, Berlin, Germany.
J Biol Inorg Chem. 2023 Jun;28(4):355-378. doi: 10.1007/s00775-023-01992-5. Epub 2023 Mar 1.
[FeFe]-hydrogenases are gas-processing metalloenzymes that catalyze H oxidation and proton reduction (H release) in microorganisms. Their high turnover frequencies and lack of electrical overpotential in the hydrogen conversion reaction has inspired generations of biologists, chemists, and physicists to explore the inner workings of [FeFe]-hydrogenase. Here, we revisit 25 years of scientific literature on [FeFe]-hydrogenase and propose a personal account on 'must-read' research papers and review article that will allow interested scientists to follow the recent discussions on catalytic mechanism, O sensitivity, and the in vivo synthesis of the active site cofactor with its biologically uncommon ligands carbon monoxide and cyanide. Focused on-but not restricted to-structural biology and molecular biophysics, we highlight future directions that may inspire young investigators to pursue a career in the exciting and competitive field of [FeFe]-hydrogenase research.
[FeFe]-氢化酶是一种气体处理金属酶，可在微生物中催化 H 氧化和质子还原（H 释放）。其高周转率和在氢转化反应中缺乏电过电势激发了一代又一代的生物学家、化学家、物理学家去探索[FeFe]-氢化酶的内部运作机制。在这里，我们重温了 25 年来关于[FeFe]-氢化酶的科学文献，并提出了一份个人的必读研究论文和综述文章清单，这将使感兴趣的科学家能够跟上最近关于催化机制、O 敏感性以及活性位点辅因子与生物中不常见配体一氧化碳和氰化物的体内合成的讨论。我们重点关注——但不限于——结构生物学和分子生物物理学，强调了可能激发年轻研究人员从事[FeFe]-氢化酶研究这一令人兴奋且竞争激烈的领域的未来方向。
