Protein secondary-shell interactions enhance the photoinduced hydrogen production of cobalt protoporphyrin IX

Dayn Joseph Sommer, Michael David Vaughn, Giovanna Ghirlanda

Research output: Contribution to journalArticlepeer-review

49 Citations (Scopus)

Abstract

Hydrogen is an attractive fuel with potential for production scalability, provided that inexpensive, efficient molecular catalysts utilizing base metals can be developed for hydrogen production. Here we show for the first time that cobalt myoglobin (CoMyo) catalyzes hydrogen production in mild aerobic conditions with turnover number of 520 over 8 hours. Compared to free Co-protoporphyrin IX, incorporation into the myoglobin scaffold results in a 4-fold increase in photoinduced hydrogen production activity. Engineered variants in which specific histidine resides in proximity of the active site were mutated to alanine result in modulation of the catalytic activity, with the H64A/H97A mutant displaying activity 2.5-fold higher than wild type. Our results demonstrate that protein scaffolds can augment and modulate the intrinsic catalytic activity of molecular hydrogen production catalysts.

Original languageEnglish
Pages (from-to)15852-15855
Number of pages4
JournalChemical Communications
Volume50
Issue number100
DOIs
Publication statusPublished - Nov 20 2014

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

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