Journal
JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY
Volume 10, Issue 2-4, Pages 181-196Publisher
KARGER
DOI: 10.1159/000091564
Keywords
[NiFe]-hydrogenases; NADH dehydrogenase; Ni-Fe-active site; metal center assembly; hydrogenase maturation; H(2) sensing; two-component system; protein complexes
Categories
Ask authors/readers for more resources
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. Copyright (c) 2005 S. Karger AG, Basel.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available