Linked Life Data

20857287

Source:http://linkedlifedata.com/resource/pubmed/id/20857287

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-1-20
pubmed:abstractText
Ferredoxin reductase BphA4 was well known as a component of biphenyl dioxygenase. However, there was little information about whether it could utilize nonphysiological oxidants as electron acceptors. In the present study, we reported the novel nitroreductase activity of BphA4(LA)??. The homology model of ferredoxin reductase BphA4 from Dyella ginsengisoli LA-4 was constructed. According to the alignment of three-dimensional structures, it was supposed that BphA4(LA)?? could function as nitroreductase. Recombinant His-tagged BphA4(LA)?? was purified with a molecular mass of 49.6?±?1 kDa. Biochemical characterization of purified BphA4(LA)?? possessed the nitroreductase activity with the optimal temperature 50°C and pH 8.0. The substrate spectrum and kinetics indicated BphA4(LA)?? could reduce several nitroaromatics with different apparent K(m) values: m-dinitrobenzene (560 ?M), o-dinitrobenzene (1,060 ?M), o-nitroaniline (1,570 ?M), m-nitrobenzoic acid (1,300 ?M) and m-nitrophenol (67 ?M). The nitroreductase activity was further explained by docking studies, which was indicated that Arg 288 should play an important role in binding nitroaromatics. Moreover, there existed a good linear correlation between lnK(m) and calculated binding energy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1432-0614
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
655-63
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Nitroreductase activity of ferredoxin reductase BphA4 from Dyella ginsengisoli LA-4 by catalytic and structural properties analysis.
pubmed:affiliation
Dalian University of Technology, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't