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

被引：28

作者：

Baker, Sarah E. ^{[1
]}

Hopkins, Robert C. ^{[2
]}

Blanchette, Craig D. ^{[1
]}

Walsworth, Vicki L. ^{[1
]}

Sumbad, Rhoda ^{[1
]}

Fischer, Nicholas O. ^{[1
]}

Kuhn, Edward A. ^{[1
]}

Coleman, Matt ^{[1
]}

Chromy, Brett A. ^{[1
]}

Letant, Sonia E. ^{[1
]}

Hoeprich, Paul D. ^{[1
]}

Adams, Michael W. W. ^{[2
]}

Henderson, Paul T. ^{[1
]}

机构：

[1] Lawrence Livermore Natl Lab, Phys & Life Sci Directorate, Livermore, CA USA

[2] Univ Georgia, Dept Biochem, Athens, GA 30602 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 22期

关键词：

IMMOBILIZATION; BIOHYDROGEN; NANODISCS; PROTEINS;

D O I：

10.1021/ja809251f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：7508 / +

页数：4

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