Laboratoire d'Energétique Macroscopique et Moléculaire, Combustion (EM2C), CNRS/CentraleSupélec, University of Paris-Saclay, Gif-sur-Yvette, France.
SETI Institute, Mountain View, California.
Biophys J. 2023 Apr 18;122(8):1557-1567. doi: 10.1016/j.bpj.2023.03.027. Epub 2023 Mar 23.
[FeFe] hydrogenases are enzymes that have acquired a unique capacity to synthesize or consume molecular hydrogen (H). This function relies on a complex catalytic mechanism involving the active site and two distinct electron and proton transfer networks working in concert. By an analysis based on terahertz vibrations of [FeFe] hydrogenase structure, we are able to predict and identify the existence of rate-promoting vibrations at the catalytic site and the coupling with functional residues involved in reported electron and proton transfer networks. Our findings suggest that the positioning of the cluster is influenced by the response of the scaffold to thermal fluctuations, which in turn drives the formation of networks for electron transfer through phonon-assisted mechanisms. Thus, we address the problem of linking the molecular structure to the catalytic function through picosecond dynamics, while raising the functional gain brought by the cofactors or clusters, using the concept of fold-encoded localized vibrations.
[FeFe]氢化酶是一种能够合成或消耗氢气（H）的酶。这种功能依赖于一个复杂的催化机制，涉及活性位点和两个不同的电子和质子转移网络协同工作。通过对[FeFe]氢化酶结构的太赫兹振动分析，我们能够预测和识别催化位点的促进反应的振动的存在，并与涉及报道的电子和质子转移网络的功能残基耦合。我们的研究结果表明，团簇的定位受到支架对热波动响应的影响，这反过来又通过声子辅助机制驱动电子转移网络的形成。因此，我们通过皮秒动力学解决了将分子结构与催化功能联系起来的问题，同时利用折叠编码局部振动的概念提高了辅助因子或团簇带来的功能增益。
