Premium
Enhanced Photocatalytic Hydrogen Production by Hybrid Streptavidin‐Diiron Catalysts
Author(s) -
Roy Anindya,
Vaughn Michael D.,
Tomlin John,
Booher Garrett J.,
Kodis Gerdenis,
Simmons Chad R.,
Allen James P.,
Ghirlanda Giovanna
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202000204
Subject(s) - streptavidin , catalysis , biotinylation , chemistry , electrocatalyst , photocatalysis , photochemistry , hydrogenase , combinatorial chemistry , spectroscopy , fourier transform infrared spectroscopy , diffuse reflectance infrared fourier transform , hydrogen production , chemical engineering , biotin , electrochemistry , organic chemistry , biochemistry , quantum mechanics , physics , electrode , engineering
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 Fe I Fe 0 when incorporated within streptavidin compared to the biotinylated catalyst in solution.