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Genome sequence of the bioplastic-producing “Knallgas” bacterium Ralstonia eutropha H16
- A. Pohlmann, W. F. Fricke, +13 authors B. Bowien
- Biology, Medicine
- Nature Biotechnology
- 10 September 2006
The complete genome sequence of the two chromosomes of R. eutropha H16 is reported, offering the genetic basis for exploiting the biotechnological potential of this organism and providing insights into its remarkable metabolic versatility. Expand
The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha.
In vitro experiments clearly demonstrated binding of PhaP2 to the poly(3HB) granules in the cells and these new and unexpected findings should affect current models of PHA-granule structure and may also have a considerable impact on the establishment of heterologous production systems for PHAs. Expand
Complete Nucleotide Sequence of pHG1: A Ralstonia eutropha H16 Megaplasmid Encoding Key Enzymes of H2-based Lithoautotrophy and Anaerobiosis
The complete nucleotide sequence of pHG1 is determined and the genes for conjugative plasmid transfer predict that R. eutropha forms two types of pili, related to the type IV pili of pathogenic enterobacteria. Expand
The Soluble NAD+-Reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 Consists of Six Subunits and Can Be Specifically Activated by NADPH
- T. Burgdorf, E. van der Linden, +7 authors B. Friedrich
- Chemistry, Biology
- Journal of bacteriology
- 1 May 2005
A new high-molecular-weight form of the SH which contains an additional subunit which suggests that HoxI provides a binding domain for NADPH, adding to the list of similarities between the SH and mitochondrial NADH:ubiquinone oxidoreductase (Complex I). Expand
Molecular biology of hydrogen utilization in aerobic chemolithotrophs.
Maturation of both types of hydrogenase is apparently complex, involving specific nickel incorporation and proteolytic processing steps, and in Alcaligenes eutrophus and Rhodobacter capsulatus, hydrogenase expression is regulated by transcriptional activators belonging to the response-regulator family. Expand
Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16
- R. A. Siddiqui, U. Warnecke-Eberz, A. Hengsberger, B. Schneider, S. Kostka, B. Friedrich
- Medicine, Biology
- Journal of bacteriology
- 1 September 1993
An insertion in the napA gene led to a complete loss of NAP activity but did not abolish the ability of A. eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration, suggesting a role for NAP in the adaptation to an aerobic metabolism. Expand
Naturally occurring genetic transfer of hydrogen-oxidizing ability between strains of Alcaligenes eutrophus
The results allow the conclusion that A. eutrophus H16 harbors a self-transmissible plasmid designated pHG1, which carries information for hydrogen-oxidizing ability, and that spontaneous Aut- mutants obtained only with strain TF93 were obtained. Expand
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution.
The molecular structure of the bacterial globin structure from those of other species is the movement of helix E in a way to provide more space in the vicinity of the distal heme binding site. Expand
The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre
The crystal structure of an O2-tolerant [Ni Fe]-hydrogenase from the aerobic H2 oxidizer Ralstonia eutropha H16 is presented and a network of extended water cavities that may act as a channel facilitating the removal of water produced at the [NiFe] active site are presented. Expand
A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.
- Tobias Goris, Annemarie F. Wait, +8 authors O. Lenz
- Chemistry, Medicine
- Nature chemical biology
- 1 May 2011
The data indicate that the mechanism of O(2) tolerance relies on the reductive removal of oxygenic species guided by the unique architecture of the electron relay rather than a restricted access of O (2) to the active site. Expand