Hydrogen production by a hyperthermophilic membrane-bound hydrogenase in water-soluble nanolipoprotein particles

Sarah E. Baker, Robert C. Hopkins, Craig D. Blanchette, Vicki L. Walsworth, Rhoda Sumbad, Nicholas O Fischer, Edward A. Kuhn, Matthew A Coleman, Brett A. Chromy, Sonia E. Létant, Paul D. Hoeprich, Michael W W Adams, Paul Henderson

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

(Chemical Equation Presented) Hydrogenases constitute a promising class of enzymes for ex vivo hydrogen production. Implementation of such applications is currently hindered by oxygen sensitivity and, in the case of membrane-bound hydrogenases (MBHs), poor water solubility. Nanolipoprotein particles (NLPs) formed from apolipoproteins and phospholipids offer a novel means of incorporating MBHs into a well-defined water-soluble matrix that maintains the enzymatic activity and is amenable to incorporation into more complex architectures. We report the synthesis, hydrogen-evolving activity, and physical characterization of the first MBH-NLP assembly. This may ultimately lead to the development of biomimetic hydrogen-production devices.

Original languageEnglish (US)
Pages (from-to)7508-7509
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number22
DOIs
StatePublished - Jun 10 2009

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

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    Baker, S. E., Hopkins, R. C., Blanchette, C. D., Walsworth, V. L., Sumbad, R., Fischer, N. O., Kuhn, E. A., Coleman, M. A., Chromy, B. A., Létant, S. E., Hoeprich, P. D., Adams, M. W. W., & Henderson, P. (2009). Hydrogen production by a hyperthermophilic membrane-bound hydrogenase in water-soluble nanolipoprotein particles. Journal of the American Chemical Society, 131(22), 7508-7509. https://doi.org/10.1021/ja809251f