Morra Simone, Arizzi Mariaconcetta, Valetti Francesca, Gilardi Gianfranco
Department of Life Sciences and Systems Biology, University of Torino , Via Accademia Albertina 13, Torino 10123, Italy.
Biochemistry. 2016 Oct 25;55(42):5897-5900. doi: 10.1021/acs.biochem.6b00780. Epub 2016 Oct 17.
The newly isolated Clostridium beijerinckii [FeFe]-hydrogenase CbA5H was characterized by Fourier transform infrared spectroscopy coupled to enzymatic activity assays. This showed for the first time that in this enzyme the oxygen-sensitive active state H can be simply and reversibly converted to the oxygen-stable inactive H state. This suggests that oxygen sensitivity is not an intrinsic feature of the catalytic center of [FeFe]-hydrogenases (H-cluster), opening new challenging perspectives on the oxygen sensitivity mechanism as well as new possibilities for exploitation in industrial applications.
新分离出的拜氏梭菌[FeFe]-氢化酶CbA5H通过傅里叶变换红外光谱结合酶活性测定进行了表征。这首次表明，在这种酶中，对氧敏感的活性状态H可以简单且可逆地转化为对氧稳定的无活性H状态。这表明氧敏感性并非[FeFe]-氢化酶（H-簇）催化中心的固有特征，为氧敏感性机制开辟了新的具有挑战性的研究视角，也为工业应用中的开发提供了新的可能性。
