A hydrogen-sensing multiprotein complex controls aerobic hydrogen metabolism in Ralstonia eutropha. (1st February 2005)

• Record Type: Journal Article
• Authors: Friedrich, B.; Buhrke, T.; Burgdorf, T.; Lenz, O.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 1(2005)
• Page Start: 97
• Page End: 101
• Publication Date: 2005-02-01
• Subjects: hydrogen metabolism -- molecular hydrogen Ralstonia eutropha -- regulatory hydrogenase -- regulatory hydrogenase–HoxJ complex -- signal transduction; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0330097
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : 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.