Reengineering cyt b562 for hydrogen production: A facile route to artificial hydrogenases

Dayn Joseph Sommer, Michael David Vaughn, Brett Colby Clark, John Tomlin, Anindya Roy, Giovanna Ghirlanda

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

Bioinspired, protein-based molecular catalysts utilizing base metals at the active are emerging as a promising avenue to sustainable hydrogen production. The protein matrix modulates the intrinsic reactivity of organometallic active sites by tuning second-sphere and long-range interactions. Here, we show that swapping Co-Protoporphyrin IX for Fe-Protoporphyrin IX in cytochrome b562 results in an efficient catalyst for photoinduced proton reduction to molecular hydrogen. Further, the activity of wild type Co-cyt b562 can be modulated by a factor of 2.5 by exchanging the coordinating methionine with alanine or aspartic acid. The observed turnover numbers (TON) range between 125 and 305, and correlate well with the redox potential of the Co-cyt b562 mutants. The photosensitized system catalyzes proton reduction with high efficiency even under an aerobic atmosphere, implicating its use for biotechnological applications. This article is part of a Special Issue entitled Biodesign for Bioenergetics - the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.

Original languageEnglish (US)
Pages (from-to)598-603
Number of pages6
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1857
Issue number5
DOIs
StatePublished - May 1 2016

Keywords

  • Cobalt catalysts
  • Fuel production
  • Protein engineering
  • Redox chemistry

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology

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