Cobaloxime-based artificial hydrogenases

Marine Bacchi, Gustav Berggren, Jens Niklas, Elias Veinberg, Michael W. Mara, Megan L. Shelby, Oleg G. Poluektov, Lin X. Chen, David M. Tiede, Christine Cavazza, Martin J. Field, Marc Fontecave, Vincent Artero*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

75 Scopus citations


Cobaloximes are popular H2 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(dmgBF2)2} (dmgH2 = 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 H2 evolution in near-neutral aqueous conditions.

Original languageEnglish (US)
Pages (from-to)8071-8082
Number of pages12
JournalInorganic chemistry
Issue number15
StatePublished - Aug 4 2014

ASJC Scopus subject areas

  • Inorganic Chemistry
  • Physical and Theoretical Chemistry


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