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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-3-25
pubmed:databankReference
pubmed:abstractText
Hydrogenase from a hot spring bacterium Klebsiella oxytoca HP1 was purified and found to have a specific activity of 199.8 U/mg of protein and a yield of 7.3%. The purified enzyme was determined to consist of six subunits (65, 33, 28, 23, 21 and 18 kDa), similar to hydrogenase-3 from Escherichia coli, and therefore it was named Hyd3. The enzyme displayed remarkable oxygen tolerance. For the purified enzyme, 50% maximal activity was maintained following incubation for 24 h in air at room temperature. The hydrogenase gene cluster (hyc) was cloned and found to consist of hycD, hycE, hycF, hycdG, hycH and hycI genes. hycE and hycG genes encode for the large and small subunit of the hydrogenase, respectively. A hycE gene deletion mutant, ?hycE, was constructed for elucidating the function of the hyc-operon in hydrogen metabolism. Compared with the wild type strain HP1, the mutant strain showed a dramatic decrease in hydrogen production in the presence of formate, sodium pyruvate and glucose under O(2)-stressed conditions, while substantial activity was detected under anaerobic conditions. This strongly suggests that K. oxytoca HP1 carries a number of hydrogenases or hydrogen metabolic pathways independently of Hyd3. However, Hyd3 is the main factor responsible for hydrogen production under O(2) stress conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1769-7123
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Institut Pasteur. Published by Elsevier SAS. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
330-6
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Characterization and cloning of oxygen-tolerant hydrogenase from Klebsiella oxytoca HP1.
pubmed:affiliation
School of Life Sciences, School of Energy Research, Xiamen University, Xiamen 361005, PR China. wuqiu01@yahoo.com.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't