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          Institute: MPI für bioanorganische Chemie     Collection: MPI für bioanorganische Chemie     Display Documents



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ID: 676743.0, MPI für bioanorganische Chemie / MPI für bioanorganische Chemie
Biomimetic assembly and activation of [FeFe]-hydrogenases
Authors:Berggren, G.; Adamska, Agnieszka; Lambertz, Camilla; Simmons, Trevor R.; Esselborn, J.; Atta, M.; Gambarelli, S.; Mouesca, J. M.; Reijerse, Edward J.; Lubitz, Wolfgang; Happe, Thomas; Artero, Vincent; Fontecave, M.
Language:English
Date of Publication (YYYY-MM-DD):2013
Title of Journal:Nature
Volume:499
Issue / Number:7456
Start Page:66
End Page:69
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Hydrogenases are the most active molecular catalysts for hydrogen production and uptake(1,2), and could therefore facilitate the development of new types of fuel cell(3-5). In [FeFe]-hydrogenases, catalysis takes place at a unique di-iron centre (the [2Fe] subsite), which contains a bridging dithiolate ligand, three CO ligands and two CN- ligands(6,7). Through a complex multienzymatic biosynthetic process, this [2Fe] subsite is first assembled on a maturation enzyme, HydF, and then delivered to the apo-hydrogenase for activation(8). Synthetic chemistry has been used to prepare remarkably similar mimics of that subsite(1), but it has failed to reproduce the natural enzymatic activities thus far. Here we show that three synthetic mimics (containing different bridging dithiolate ligands) can be loaded onto bacterial Thermotoga maritima HydF and then transferred to apo-HydA1, one of the hydrogenases of Chlamy-domonas reinhardtii algae. Full activation of HydA1 was achieved only when using the HydF hybrid protein containing the mimic with an azadithiolate bridge, confirming the presence of this ligand in the active site of native [FeFe]-hydrogenases(9,10). This is an example of controlled metalloenzyme activation using the combination of a specific protein scaffold and active-site synthetic analogues. This simple methodology provides both new mechanistic and structural insight into hydrogenase maturation and a unique tool for producing recombinant wild-type and variant [FeFe]-hydrogenases, with no requirement for the complete maturation machinery.
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für bioanorganische Chemie
External Affiliations:Berggren, G.; Simmons, T. R.; Atta, M.; Artero, V.; Fontecave, M.; Univ Grenoble 1, CNRS, CEA, Lab Chim & Biol Met, F-38054 Grenoble 9, France.
Lambertz, C.; Esselborn, J.; Happe, T.; Ruhr Univ Bochum, AG Photobiotechnol, Lehrstuhl Biochem Pflanzen, D-44801 Bochum, Germany.
Gambarelli, S.; Mouesca, J. -M.;Univ Grenoble 1, CEA INAC, Lab Chim Inorgan & Biol, UMR E 3, F-38054 Grenoble 9, France.
Identifiers:ISI:000321285600034 [ID No:1]
ISSN:0028-0836 [ID No:2]
DOI:10.1038/nature12239 [ID No:3]
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