Journal
INORGANIC CHEMISTRY
Volume 53, Issue 15, Pages 8071-8082Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ic501014c
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Funding
- French National Research Agency (ANR, NiFe-Cat project) [ANR-10-BLAN-711,]
- French National Research Agency (ANR, Labex program ARCANE) [ANR-11-LABX-0003-01]
- COST Action [CM1202 PERSPECT-H2O]
- Life Science Division of the CEA (Irtelis program)
- Life Science Division of the CEA (DSV-Energy program)
- Bengt Lundqvist minnesfond
- FORMAS [213-2010-563]
- Swedish Royal Academy of Sciences
- Division of Chemical Sciences, Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-AC02-06CH11357]
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Cobaloximes are popular H-2 evolution molecular catalysts but have so far mainly been studied in nonaqueous conditions. We show here that they are also valuable for the design of artificial hydrogenases for application in neutral aqueous solutions and report on the preparation of two well-defined biohybrid species via the binding of two cobaloxime moieties, {Co(dmgH)(2)} and {Co(dmgBF(2))(2)} (dmgH(2) = dimethylglyoxime), to apo Sperm-whale myoglobin (SwMb). All spectroscopic data confirm that the cobaloxime moieties are inserted within the binding pocket of the SwMb protein and are coordinated to a histidine residue in the axial position of the cobalt complex, resulting in thermodynamically stable complexes. Quantum chemical/molecular mechanical docking calculations indicated a coordination preference for His93 over the other histidine residue (His64) present in the vicinity. Interestingly, the redox activity of the cobalt centers is retained in both biohybrids, which provides them with the catalytic activity for H-2 evolution near-neutral aqueous conditions. in
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