Burgdorf Tanja, Lenz Oliver, Buhrke Thorsten, van der Linden Eddy, Jones Anne K, Albracht Simon P J, Friedrich Bärbel
Institut für Biologie, Humboldt-Universität zu Berlin, Berlin, Germany.
J Mol Microbiol Biotechnol. 2005;10(2-4):181-96. doi: 10.1159/000091564.
Recent research on hydrogenases has been notably motivated by a desire to utilize these remarkable hydrogen oxidation catalysts in biotechnological applications. Progress in the development of such applications is substantially hindered by the oxygen sensitivity of the majority of hydrogenases. This problem tends to inspire the study of organisms such as Ralstonia eutropha H16 that produce oxygen-tolerant [NiFe]-hydrogenases. R. eutropha H16 serves as an excellent model system in that it produces three distinct [NiFe]-hydrogenases that each serve unique physiological roles: a membrane-bound hydrogenase (MBH) coupled to the respiratory chain, a cytoplasmic, soluble hydrogenase (SH) able to generate reducing equivalents by reducing NAD+ at the expense of hydrogen, and a regulatory hydrogenase (RH) which acts in a signal transduction cascade to control hydrogenase gene transcription. This review will present recent results regarding the biosynthesis, regulation, structure, activity, and spectroscopy of these enzymes. This information will be discussed in light of the question how do organisms adapt the prototypical [NiFe]-hydrogenase system to function in the presence of oxygen.
近期对氢化酶的研究主要是受在生物技术应用中利用这些卓越的氢氧化催化剂这一愿望的推动。大多数氢化酶对氧气敏感，这在很大程度上阻碍了此类应用的开发进展。这个问题促使人们去研究诸如真养产碱杆菌H16等能产生耐氧[NiFe] - 氢化酶的生物体。真养产碱杆菌H16是一个出色的模型系统，因为它能产生三种不同的[NiFe] - 氢化酶，每种都发挥独特的生理作用：一种与呼吸链偶联的膜结合氢化酶（MBH）、一种能够通过以氢气为代价还原NAD⁺来产生还原当量的细胞质可溶性氢化酶（SH），以及一种在信号转导级联反应中起作用以控制氢化酶基因转录的调节性氢化酶（RH）。本综述将介绍有关这些酶的生物合成、调控、结构、活性和光谱学的最新研究结果。将根据生物体如何使原型[NiFe] - 氢化酶系统在有氧环境中发挥作用这一问题来讨论这些信息。
