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. 2009 Jun 10;131(22):7508-9.
doi: 10.1021/ja809251f.

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

Sarah E Baker  1 , Robert C Hopkins, Craig D Blanchette, Vicki L Walsworth, Rhoda Sumbad, Nicholas O Fischer, Edward A Kuhn, Matt Coleman, Brett A Chromy, Sonia E Létant, Paul D Hoeprich, Michael W W Adams, Paul T Henderson
Affiliations

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

Sarah E Baker et al. J Am Chem Soc. .

Abstract

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.

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