期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 131, 期 22, 页码 7508-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja809251f
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资金
- U.S. Department of Energy by Lawrence Livermore National Laboratory [DE-AC52-07NA27344]
- Lawrence Livermore National Laboratory [LDRD 06-SI-003]
- U.S. DOE [DE-FG02-05ER15710]
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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