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Structure, function and biosynthesis of O(2)-tolerant hydrogenases.
MedLine Citation:
PMID:  23321533     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Molecular hydrogen (H(2)) is used as an energy source or a way to deposit excess reducing power by a wide range of microorganisms. Both H(2) oxidation and production are catalysed by hydrogenases. As these metalloenzymes are usually exquisitely O(2) sensitive, H(2) metabolism under aerobic conditions, which is known as O(2)-tolerant H(2) cycling, involves hydrogenases that have undergone structural and catalytic adaptations and requires a dedicated biosynthetic machinery. Here, we discuss recent high-resolution crystal structure analyses of a particular subtype of [NiFe]-hydrogenase that is predominantly found in aerobic or facultative aerobic H(2)-oxidizing bacteria. These data have provided insights into the underlying molecular strategies that allow sustained biological conversion of H(2) in the presence of O(2).
Authors:
Johannes Fritsch; Oliver Lenz; Bärbel Friedrich
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Nature reviews. Microbiology     Volume:  11     ISSN:  1740-1534     ISO Abbreviation:  Nat. Rev. Microbiol.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101190261     Medline TA:  Nat Rev Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  106-14     Citation Subset:  IM    
Affiliation:
Mikrobiologie, Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestraße 117, 10115 Berlin, Germany.
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