title: [NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation.
abstract: Recent research on hydrogenases has been notably motivated by a desire to utilize these remarkable hydrogen oxidation catalysts in biotechnological applications. Progress in the development of such applications is substantially hindered by the oxygen sensitivity of the majority of hydrogenases. This problem tends to inspire the study of organisms such as Ralstonia eutropha H16 that produce oxygen-tolerant [NiFe]-hydrogenases. R. eutropha H16 serves as an excellent model system in that it produces three distinct [NiFe]-hydrogenases that each serve unique physiological roles: a membrane-bound hydrogenase (MBH) coupled to the respiratory chain, a cytoplasmic, soluble hydrogenase (SH) able to generate reducing equivalents by reducing NAD+ at the expense of hydrogen, and a regulatory hydrogenase (RH) which acts in a signal transduction cascade to control hydrogenase gene transcription. This review will present recent results regarding the biosynthesis, regulation, structure, activity, and spectroscopy of these enzymes. This information will be discussed in light of the question how do organisms adapt the prototypical [NiFe]-hydrogenase system to function in the presence of oxygen.
authors.affiliation: Institut für Biologie, Humboldt-Universität zu Berlin, Berlin, Germany.
authors.forename: Tanja
authors.initials: T
authors.lastname: Burgdorf
authors.forename: Oliver
authors.initials: O
authors.lastname: Lenz
authors.forename: Thorsten
authors.initials: T
authors.lastname: Buhrke
authors.forename: Eddy
authors.initials: E
authors.lastname: van der Linden
authors.forename: Anne K
authors.initials: AK
authors.lastname: Jones
authors.forename: Simon P J
authors.initials: SP
authors.lastname: Albracht
authors.forename: Bärbel
authors.initials: B
authors.lastname: Friedrich
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D020118:Cupriavidus necator / Q000201:enzymology*; D006859:Hydrogen / Q000378:metabolism*; D006864:Hydrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D006859:Hydrogen; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D011494:Protein Kinases; C104634:HoxJ protein, bacteria; D010100:Oxygen