Enhanced Photocatalytic Hydrogen Production by Hybrid Streptavidin-Diiron Catalysts

Anindya Roy, Michael D. Vaughn, John Tomlin, Garrett J. Booher, Gerdenis Kodis, Chad R. Simmons, James P. Allen, Giovanna Ghirlanda

Research output: Contribution to journalArticle

Abstract

Hybrid protein–organometallic catalysts are being explored for selective catalysis of a number of reactions, because they utilize the complementary strengths of proteins and of organometallic complex. Herein, we present an artificial hydrogenase, StrepH2, built by incorporating a biotinylated [Fe–Fe] hydrogenase organometallic mimic within streptavidin. This strategy takes advantage of the remarkable strength and specificity of biotin-streptavidin recognition, which drives quantitative incorporation of the biotinylated diironhexacarbonyl center into streptavidin, as confirmed by UV/Vis spectroscopy and X-ray crystallography. FTIR spectra of StrepH2 show characteristic peaks at shift values indicative of interactions between the catalyst and the protein scaffold. StrepH2 catalyzes proton reduction to hydrogen in aqueous media during photo- and electrocatalysis. Under photocatalytic conditions, the protein-embedded catalyst shows enhanced efficiency and prolonged activity compared to the isolated catalyst. Transient absorption spectroscopy data suggest a mechanism for the observed increase in activity underpinned by an observed longer lifetime for the catalytic species FeIFe0 when incorporated within streptavidin compared to the biotinylated catalyst in solution.

Original languageEnglish (US)
Pages (from-to)6240-6246
Number of pages7
JournalChemistry - A European Journal
Volume26
Issue number28
DOIs
StatePublished - May 15 2020

Keywords

  • X-ray crystallography
  • catalysis
  • hybrid enzymes
  • hydrogen production
  • streptavidin-avidin

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry

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