Hydrogen Production by a Hyperthermophilic Membrane-Bound Hydrogenase in Soluble Nanolipoprotein Particles

Journal Article · Wed Oct 22 00:00:00 EDT 2008 · Journal of the American Chemical Society

OSTI ID:964089

Baker, S E; Hopkins, R C; Blanchette, C; Walsworth, V; Sumbad, R; Fischer, N; Kuhn, E; Coleman, M; Chromy, B; Letant, S; Hoeprich, P; Adams, M W; Henderson, P T

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 (MBH), poor water solubility. Nanolipoprotein particles (NLPs), formed from apolipoproteins and phospholipids, offer a novel means to incorporate MBH into in 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.

• Research Organization: Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
• Sponsoring Organization: USDOE
• DOE Contract Number: W-7405-ENG-48
• OSTI ID: 964089
• Report Number(s): LLNL-JRNL-408807; JACSAT; TRN: US200922%%89
• Journal Information: Journal of the American Chemical Society, Vol. 131, Issue 22; ISSN 0002-7863
• Country of Publication: United States
• Language: English

Related Subjects

08 HYDROGEN
59 BASIC BIOLOGICAL SCIENCES
APOLIPOPROTEINS
ENZYMES
HYDROGEN PRODUCTION
HYDROGENASES
IMPLEMENTATION
OXYGEN
PHOSPHOLIPIDS
SENSITIVITY
SOLUBILITY
SYNTHESIS
WATER