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From Enzyme Maturation to Synthetic Chemistry: The Case of Hydrogenases
Univ Grenoble Alpes, CNRS, CEA, Lab Chem & Biol Met, F-38000 Grenoble, France..
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Univ Grenoble Alpes, CNRS, CEA, Lab Chem & Biol Met, F-38000 Grenoble, France..
Univ Paris 06, CNRS, Coll France, Lab Chim Proc Biol, F-75005 Paris, France..
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2015 (English)In: Accounts of Chemical Research, ISSN 0001-4842, E-ISSN 1520-4898, Vol. 48, no 8, 2380-2387 p.Article, review/survey (Refereed) Published
Abstract [en]

CONSPECTUS: Water splitting into oxygen and hydrogen is one of the most attractive strategies for storing solar energy and electricity. Because the processes at work are multielectronic, there is a crucial need for efficient and stable catalysts, which in addition have to be cheap for future industrial developments (electrolyzers, photoelectrochemicals, and fuel cells). Specifically for the water/hydrogen interconversion, Nature is an exquisite source of inspiration since this chemistry contributes to the bioenergetic metabolism of a number of living organisms via the activity of fascinating metalloenzymes, the hydrogenases. In this Account, we first briefly describe the structure of the unique dinuclear organometallic active sites of the two classes of hydrogenases as well as the complex protein machineries involved in their biosynthesis, their so-called maturation processes. This knowledge allows for the development of a fruitful bioinspired chemistry approach, which has already led to a number of interesting and original catalysts mimicking the natural active sites. More specifically, we describe our own attempts to prepare artificial hydrogenases. This can be achieved via the standard bioinspired approach using the combination of a synthetic bioinspired catalyst and a polypeptide scaffold. Such hybrid complexes provide the opportunity to optimize the system by manipulating both the catalyst through chemical synthesis and the protein component through mutagenesis. We also raise the possibility to reach such artificial systems via an original strategy based on mimicking the enzyme maturation pathways. This is illustrated in this Account by two examples developed in our laboratory. First, we show how the preparation of a lysozyme-{Mn-I(CO)(3)} hybrid and its clean reaction with a nickel complex led us to generate a new class of binuclear Ni-Mn H-2-evolving catalysts mimicking the active site of [NiFe]-hydrogenases. Then we describe how we were able to rationally design and prepare a hybrid system, displaying remarkable structural similarities to an [FeFe]-hydrogenase, and we show here for the first time that it is catalytically active for proton reduction. This system is based on the combination of HydF, a protein involved in the maturation of [FeFe]-hydrogenase (HydA), and a close mimic of the active site of this class of enzymes. Moreover, the synthetic [Fe-2(adt)(CO)(4)(CN)(2)](2-) (adt(2-) = aza-propanedithiol) mimic, alone or within a HydF hybrid system, was shown to be able to maturate and activate a form of HydA itself lacking its diiron active site. We discuss the exciting perspectives this "synthetic maturation" opens regarding the "invention" of novel hydrogenases by the chemists.

Place, publisher, year, edition, pages
2015. Vol. 48, no 8, 2380-2387 p.
National Category
Chemical Sciences
URN: urn:nbn:se:uu:diva-264087DOI: 10.1021/acs.accounts.5b00157ISI: 000359892700022PubMedID: 26165393OAI: oai:DiVA.org:uu-264087DiVA: diva2:859014
Swedish Research Council Formas, 213-2014-880Swedish Research Council, 621-2014-5670Magnus Bergvall Foundation
Available from: 2015-10-05 Created: 2015-10-05 Last updated: 2015-10-05Bibliographically approved

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