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J. Biol. Chem., Vol. 276, Issue 19, 15592-15597, May 11, 2001
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From the 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 paper is dedicated to Prof. Ernst-G. Jäger on the occasion
of his 65th birthday on May 5, 2001.
The H2 Sensor of Ralstonia eutropha
BIOCHEMICAL CHARACTERISTICS, SPECTROSCOPIC PROPERTIES, AND ITS
INTERACTION WITH A HISTIDINE PROTEIN KINASE*
,,
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
*
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.
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.
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