Hydrogen production by a hyperthermophilic membrane-bound hydrogenase in water-soluble nanolipoprotein particles.
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.
Baker
Sarah E
SE
Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, USA.
Hopkins
Robert C
RC
Blanchette
Craig D
CD
Walsworth
Vicki L
VL
Sumbad
Rhoda
R
Fischer
Nicholas O
NO
Kuhn
Edward A
EA
Coleman
Matt
M
Chromy
Brett A
BA
Létant
Sonia E
SE
Hoeprich
Paul D
PD
Adams
Michael W W
MW
Henderson
Paul T
PT
D001053:Apolipoproteins / Q000737:chemistry*; D002462:Cell Membrane / Q000201:enzymology; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D020027:Pyrococcus furiosus / Q000201:enzymology; D012995:Solubility; D014867:Water / Q000737:chemistry
D001053:Apolipoproteins; D004800:Enzymes, Immobilized; D010743:Phospholipids; D014867:Water; D006859:Hydrogen; D006864:Hydrogenase