[Journal Club] Une autre façon de “voir” le mécanisme des métalloenzymes
Des chercheurs marseillais décrivent comment une combinaison d’informations issues de techniques très variées (mutagenèse dirigée, DFT, MD, cinétique électrochimique) permet de mieux comprendre certains aspects très variés du mécanisme catalytique de métalloenzymes.
Some reactions which are very important in the context of energy and environment, such as the conversion between CO and CO2, or H+ and H2, are catalyzed in living organisms by large and complex enzymes that use inorganic active sites to transform substrates, chains of redox centers to transfer electrons, ionizable amino acids to transfer protons, and networks of hydrophobic cavities to guide the diffusion of substrates and products within the protein. This highly sophisticated biological plumbing and wiring makes turnover frequencies of thousands of substrate molecules per second possible. Understanding the molecular details of catalysis is still a challenge. We explain in this review how a great deal of information can be obtained using an interdisciplinary approach that combines state-of-the art kinetics and computational chemistry. This differs from — and complements — the more traditional strategies that consist in trying to see the catalytic intermediates using methods that rely on the interaction between light and matter, such as X-ray diffraction and spectroscopic techniques.
Reference: Claudio Greco, Vincent Fourmond, Carole Baffert, Po-Hung Wang, Sébastien Dementin, Patrick Bertrand, Maurizio Bruschi, Jochen Blumberger, Luca de Gioia, Christophe Léger. Energy Environ. Sci., 7, 3543-3573 (2014) Epub Sept 11 2014. DOI: 10.1039/C4EE01848F (open access)