Artificial hydrogenases

Bryan E. Barton; Matthew T. Olsen; Thomas B. Rauchfuss

doi:10.1016/j.copbio.2010.03.003

Artificial hydrogenases

Bryan E. Barton, Matthew T. Olsen, Thomas B. Rauchfuss

Chemistry

Research output: Contribution to journal › Review article › peer-review

Abstract

Decades of biophysical study on the hydrogenase (H₂ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H₂ases, [NiFe]-H₂ases, and [Fe]-H₂ases, all of which feature iron centers bound to both CO and thiolate. Artificial H₂ases affect the oxidation of H₂ and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H₂ toward biomimetic H₂ases.

Original language	English (US)
Pages (from-to)	292-297
Number of pages	6
Journal	Current Opinion in Biotechnology
Volume	21
Issue number	3
DOIs	https://doi.org/10.1016/j.copbio.2010.03.003
State	Published - Jun 2010

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biomedical Engineering

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10.1016/j.copbio.2010.03.003

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title = "Artificial hydrogenases",

abstract = "Decades of biophysical study on the hydrogenase (H2ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H2ases, [NiFe]-H2ases, and [Fe]-H2ases, all of which feature iron centers bound to both CO and thiolate. Artificial H2ases affect the oxidation of H2 and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H2 toward biomimetic H2ases.",

author = "Barton, {Bryan E.} and Olsen, {Matthew T.} and Rauchfuss, {Thomas B.}",

note = "Funding Information: The authors acknowledge support from the US Department of Energy, Office of Basic Energy Sciences and the US National Institutes of Health. ",

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AU - Olsen, Matthew T.

AU - Rauchfuss, Thomas B.

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N2 - Decades of biophysical study on the hydrogenase (H2ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H2ases, [NiFe]-H2ases, and [Fe]-H2ases, all of which feature iron centers bound to both CO and thiolate. Artificial H2ases affect the oxidation of H2 and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H2 toward biomimetic H2ases.

AB - Decades of biophysical study on the hydrogenase (H2ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H2ases, [NiFe]-H2ases, and [Fe]-H2ases, all of which feature iron centers bound to both CO and thiolate. Artificial H2ases affect the oxidation of H2 and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H2 toward biomimetic H2ases.

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Artificial hydrogenases

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