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Originally published In Press as doi:10.1074/jbc.M009802200 on February 16, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15592-15597, May 11, 2001
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The H2 Sensor of Ralstonia eutropha
BIOCHEMICAL CHARACTERISTICS, SPECTROSCOPIC PROPERTIES, AND ITS INTERACTION WITH A HISTIDINE PROTEIN KINASE*

Michael BernhardDagger , Thorsten BuhrkeDagger , Boris Bleijlevens§, Antonio L. De Lacey, Victor M. Fernandez, Simon P. J. Albracht§, and Bärbel FriedrichDagger ||

From the Dagger  Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestrasse 117, 10115 Berlin, Germany, the § Swammerdam Institute for Life Sciences, Department of Biochemistry, University of Amsterdam, Plantage Muidergracht 12, NL-1018 TV Amsterdam, The Netherlands, and the  Instituto de Catalisis, CSIC, Campus Universidad Autonoma-Cantoblanco, 28049 Madrid, Spain

Previous genetic studies have revealed a multicomponent signal transduction chain, consisting of an H2 sensor, a histidine protein kinase, and a response regulator, which controls hydrogenase gene transcription in the proteobacterium Ralstonia eutropha. In this study, we isolated the H2 sensor and demonstrated that the purified protein forms a complex with the histidine protein kinase. Biochemical and spectroscopic analysis revealed that the H2 sensor is a cytoplasmic [NiFe]-hydrogenase with unique features. The H2-oxidizing activity was 2 orders of magnitude lower than that of standard hydrogenases and insensitive to oxygen, carbon monoxide, and acetylene. Interestingly, only H2 production but no HD formation was detected in the D2/H+ exchange assay. Fourier transform infrared data showed an active site similar to that of standard [NiFe]-hydrogenases. It is suggested that the protein environment accounts for a restricted gas diffusion and for the typical kinetic parameters of the H2 sensor. EPR analysis demonstrated that the [4Fe-4S] clusters within the small subunit were not reduced under hydrogen even in the presence of dithionite. Optical spectra revealed the presence of a novel, redox-active, n = 2 chromophore that is reduced by H2. The possible involvement of this chromophore in signal transduction is discussed.


* This work was supported by the The Netherlands Organization for Scientific Research, the Deutsche Forschungsgemeinschaft, and the Fonds der Chemischen Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

This paper is dedicated to Prof. Ernst-G. Jäger on the occasion of his 65th birthday on May 5, 2001.

|| To whom correspondence should be addressed. Tel.: 49 30 20 93 81 01; Fax: 49 30 20 93 81 02; E-mail: baerbel.friedrich@rz.hu-berlin.de.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.