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Table of Contents
Vol. 10, No. 2-4, 2005
Issue release date: April 2006
Section title: Minireview
J Mol Microbiol Biotechnol 2005;10:181–196
(DOI:10.1159/000091564)

[NiFe]-Hydrogenases of Ralstonia eutropha H16: Modular Enzymes for Oxygen-Tolerant Biological Hydrogen Oxidation

Burgdorf T.a · Lenz O.a · Buhrke T.a · van der Linden E.b · Jones A.K.c · Albracht S.P.J.b · Friedrich B.a
aInstitut für Biologie, Humboldt-Universität zu Berlin, Berlin, Germany; bSwammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands; cThe Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pa., USA

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Article / Publication Details

First-Page Preview
Abstract of Minireview

Received: July 04, 2005
Accepted: November 28, 2005
Published online: April 27, 2006
Issue release date: April 2006

Number of Print Pages: 16
Number of Figures: 9
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB

Abstract

Recent research on hydrogenases has been notably motivated by a desire to utilize these remarkable hydrogen oxidation catalysts in biotechnological applications. Progress in the development of such applications is substantially hindered by the oxygen sensitivity of the majority of hydrogenases. This problem tends to inspire the study of organisms such as Ralstonia eutropha H16 that produce oxygen-tolerant [NiFe]-hydrogenases. R. eutropha H16 serves as an excellent model system in that it produces three distinct [NiFe]-hydrogenases that each serve unique physiological roles: a membrane-bound hydrogenase (MBH) coupled to the respiratory chain, a cytoplasmic, soluble hydrogenase (SH) able to generate reducing equivalents by reducing NAD+ at the expense of hydrogen, and a regulatory hydrogenase (RH) which acts in a signal transduction cascade to control hydrogenase gene transcription. This review will present recent results regarding the biosynthesis, regulation, structure, activity, and spectroscopy of these enzymes. This information will be discussed in light of the question how do organisms adapt the prototypical [NiFe]-hydrogenase system to function in the presence of oxygen.

© 2005 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Minireview

Received: July 04, 2005
Accepted: November 28, 2005
Published online: April 27, 2006
Issue release date: April 2006

Number of Print Pages: 16
Number of Figures: 9
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB


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Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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