H2 is an attractive energy source for many microorganisms and is mostly consumed before it enters oxic habitats. Thus aerobic H2-oxidizing organisms receive H2 only occasionally and in limited amounts. Metabolic adaptation requires a robust oxygen-tolerant hydrogenase enzyme system and special regulatory devices that enable the organism to respond rapidly to a changing supply of H2. The proteobacterium Ralstonia eutropha strain H16 that harbours three [NiFe] hydrogenases perfectly meets these demands. The unusual biochemical and structural properties of the hydrogenases are described, including the strategies that confer O2 tolerance to the NAD-reducing soluble hydrogenase and the H2-sensing regulatory hydrogenase. The regulatory hydrogenase that forms a complex with a histidine protein kinase recognizes H2 in the environment and transmits the signal to a response regulator, which in turn controls transcription of the hydrogenase genes.
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Conference Article|
February 01 2005
A hydrogen-sensing multiprotein complex controls aerobic hydrogen metabolism in Ralstonia eutropha
B. Friedrich;
B. Friedrich
1
1Institute of Biology, Humboldt University, Berlin, Germany
1To whom correspondence should be addressed (email baerbel.friedrich@rz.hu-berlin.de).
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T. Buhrke;
T. Buhrke
1Institute of Biology, Humboldt University, Berlin, Germany
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T. Burgdorf;
T. Burgdorf
1Institute of Biology, Humboldt University, Berlin, Germany
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O. Lenz
O. Lenz
1Institute of Biology, Humboldt University, Berlin, Germany
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Publisher: Portland Press Ltd
Received:
September 30 2004
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2005 The Biochemical Society
2005
Biochem Soc Trans (2005) 33 (1): 97–101.
Article history
Received:
September 30 2004
Citation
B. Friedrich, T. Buhrke, T. Burgdorf, O. Lenz; A hydrogen-sensing multiprotein complex controls aerobic hydrogen metabolism in Ralstonia eutropha. Biochem Soc Trans 1 February 2005; 33 (1): 97–101. doi: https://doi.org/10.1042/BST0330097
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