Mimicking hydrogenases: From biomimetics to artificial enzymes
2014 (English)In: Coordination chemistry reviews, ISSN 0010-8545, E-ISSN 1873-3840, Vol. 270, 127-150 p.Article, review/survey (Refereed) Published
Over the last 15 years, a plethora of research has provided major insights into the structure and function of hydrogenase enzymes. This has led to the important development of chemical models that mimic the inorganic enzymatic co-factors, which in turn has further contributed to the understanding of the specific molecular features of these natural systems that facilitate such large and robust enzyme activities. More recently, efforts have been made to generate guest-host models and artificial hydrogenases, through the incorporation of transition metal-catalysts (guests) into various hosts. This adds a new layer of complexity to hydrogenase-like catalytic systems that allows for better tuning of their activity through manipulation of both the first (the guest) and the second (the host) coordination spheres. Herein we review the aforementioned advances achieved during the last 15 years, in the field of inorganic biomimetic hydrogenase chemistry. After a brief presentation of the enzymes themselves, as well as the early bioinspired catalysts, we review the more recent systems constructed as models for the hydrogenase enzymes, with a specific focus on the various strategies employed for incorporating of synthetic models into supramolecular frameworks and polypeptidic/protein scaffolds, and critically discuss the advantages of such an elaborate approach, with regard to the catalytic performances.
Place, publisher, year, edition, pages
2014. Vol. 270, 127-150 p.
Hydrogen, Hydrogenase, Biomimetic chemistry, Bioinspired chemistry, Artificial enzyme, Biohybrids, Photocatalysis, Electrocatalysis
IdentifiersURN: urn:nbn:se:su:diva-105401DOI: 10.1016/j.ccr.2013.12.018ISI: 000336013800009OAI: oai:DiVA.org:su-105401DiVA: diva2:728943