NAD(H)-coupled hydrogen cycling - Structure-function relationships of bidirectional [NiFe] hydrogenases

M. Horch; L. Lauterbach; O. Lenz; P. Hildebrandt; I. Zebger

doi:10.1016/j.febslet.2011.10.010

NAD(H)-coupled hydrogen cycling - Structure-function relationships of bidirectional [NiFe] hydrogenases

M. Horch, L. Lauterbach, O. Lenz, P. Hildebrandt, I. Zebger^*

^*Corresponding author for this work

Chemistry

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

Abstract

Hydrogenases catalyze the activation or production of molecular hydrogen. Due to their potential importance for future biotechnological applications, these enzymes have been in the focus of intense research for the past decades. Bidirectional [NiFe] hydrogenases are of particular interest as they couple the reversible cleavage of hydrogen to the redox conversion of NAD(H). In this account, we review the current state of knowledge about mechanistic aspects and structural determinants of these complex multi-cofactor enzymes. Special emphasis is laid on the oxygen-tolerant NAD(H)-linked bidirectional [NiFe] hydrogenase from Ralstonia eutropha.

Original language	English
Pages (from-to)	545-556
Number of pages	12
Journal	FEBS Letters
Volume	586
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2011.10.010
Publication status	Published - 9 Mar 2012

Keywords

Biocatalysis
Biofuel
Hydrogenase
NADH regeneration
Oxygen tolerance
Spectroscopy

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10.1016/j.febslet.2011.10.010

https://doi.org/10.1016/j.febslet.2011.10.010Licence: CC BY-NC-ND

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title = "NAD(H)-coupled hydrogen cycling - Structure-function relationships of bidirectional [NiFe] hydrogenases",

abstract = "Hydrogenases catalyze the activation or production of molecular hydrogen. Due to their potential importance for future biotechnological applications, these enzymes have been in the focus of intense research for the past decades. Bidirectional [NiFe] hydrogenases are of particular interest as they couple the reversible cleavage of hydrogen to the redox conversion of NAD(H). In this account, we review the current state of knowledge about mechanistic aspects and structural determinants of these complex multi-cofactor enzymes. Special emphasis is laid on the oxygen-tolerant NAD(H)-linked bidirectional [NiFe] hydrogenase from Ralstonia eutropha.",

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author = "M. Horch and L. Lauterbach and O. Lenz and P. Hildebrandt and I. Zebger",

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AU - Horch, M.

AU - Lauterbach, L.

AU - Lenz, O.

AU - Hildebrandt, P.

AU - Zebger, I.

PY - 2012/3/9

Y1 - 2012/3/9

N2 - Hydrogenases catalyze the activation or production of molecular hydrogen. Due to their potential importance for future biotechnological applications, these enzymes have been in the focus of intense research for the past decades. Bidirectional [NiFe] hydrogenases are of particular interest as they couple the reversible cleavage of hydrogen to the redox conversion of NAD(H). In this account, we review the current state of knowledge about mechanistic aspects and structural determinants of these complex multi-cofactor enzymes. Special emphasis is laid on the oxygen-tolerant NAD(H)-linked bidirectional [NiFe] hydrogenase from Ralstonia eutropha.

AB - Hydrogenases catalyze the activation or production of molecular hydrogen. Due to their potential importance for future biotechnological applications, these enzymes have been in the focus of intense research for the past decades. Bidirectional [NiFe] hydrogenases are of particular interest as they couple the reversible cleavage of hydrogen to the redox conversion of NAD(H). In this account, we review the current state of knowledge about mechanistic aspects and structural determinants of these complex multi-cofactor enzymes. Special emphasis is laid on the oxygen-tolerant NAD(H)-linked bidirectional [NiFe] hydrogenase from Ralstonia eutropha.

KW - Biocatalysis

KW - Biofuel

KW - Hydrogenase

KW - NADH regeneration

KW - Oxygen tolerance

KW - Spectroscopy

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DO - 10.1016/j.febslet.2011.10.010

M3 - Review article

C2 - 22056977

AN - SCOPUS:84857915091

SN - 0014-5793

VL - 586

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EP - 556

JO - FEBS Letters

JF - FEBS Letters

IS - 5

ER -

NAD(H)-coupled hydrogen cycling - Structure-function relationships of bidirectional [NiFe] hydrogenases

Abstract

Keywords

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