Eighth paper from a Short-Term Scientific Mission (STSM) (July 18, 2016)
This collaborative project between several research groups involves two groups of ECOSTBio: Carole Duboc (Grenoble Alpes University, France) and Franc Meyer (University of Göttingen, Germany)
This work has been recently awarded during the last Hydrogenase conference in Marseilles via a special poster prize for the PhD student Deborah Brazzolotto.
Hydrogen production through water splitting is one of the most promising solutions for the storage of renewable energy. [NiFe] hydrogenases are organometallic enzymes containing nickel and iron centers that catalyze hydrogen evolution with performances that rival those of platinum. These enzymes provide inspiration for the design of new molecular catalysts that do not require precious metals. However, all heterodinuclear NiFe models reported so far do not reproduce the Ni-centered reactivity found at the active site of [NiFe] hydrogenases. Here we report a structural and functional NiFe mimic that displays reactivity at the Ni site. This is shown by the detection of two catalytic intermediates that reproduce structural and electronic features of the Ni-L and Ni-R states of the enzyme during catalytic turnover. Under electrocatalytic conditions, this mimic displays high rates for H2 evolution (second order rate constant of 2.5 104 M-1s-1; turnover frequency of 250 s-1 at 10 mM H+ concentration) from mildly acidic solutions.
This work has been recently awarded during the last Hydrogenase conference in Marseilles via a special poster prize for the PhD student Deborah Brazzolotto, involved in the STSM.
STSM reference: COST-STSM-CM1305-26539
STSM Participant: Deborah Brazzolotto
D. Brazzolotto, M. Gennari, N. Queyriaux, T.R. Simmons, J. Pécaut, S. Demeshko, F. Meyer, M. Orio, V. Artero, and C. Duboc
"Nickel-centred proton reduction catalysis in a model of [NiFe] hydrogenase"
Nature Chem 2016, 8, 1054-1060