Linked Life Data

12051836

Source:http://linkedlifedata.com/resource/pubmed/id/12051836

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-6-7
pubmed:databankReference
pubmed:abstractText
One of the major processes for aerobic biodegradation of aromatic compounds is initiated by Rieske dioxygenases. Benzoate dioxygenase contains a reductase component, BenC, that is responsible for the two-electron transfer from NADH via FAD and an iron-sulfur cluster to the terminal oxygenase component. Here, we present the structure of BenC from Acinetobacter sp. strain ADP1 at 1.5 A resolution. BenC contains three domains, each binding a redox cofactor: iron-sulfur, FAD and NADH, respectively. The [2Fe-2S] domain is similar to that of plant ferredoxins, and the FAD and NADH domains are similar to members of the ferredoxin:NADPH reductase superfamily. In phthalate dioxygenase reductase, the only other Rieske dioxygenase reductase for which a crystal structure is available, the ferredoxin-like and flavin binding domains are sequentially reversed compared to BenC. The BenC structure shows significant differences in the location of the ferredoxin domain relative to the other domains, compared to phthalate dioxygenase reductase and other known systems containing these three domains. In BenC, the ferredoxin domain interacts with both the flavin and NAD(P)H domains. The iron-sulfur center and the flavin are about 9 A apart, which allows a fast electron transfer. The BenC structure is the first determined for a reductase from the class IB Rieske dioxygenases, whose reductases transfer electrons directly to their oxygenase components. Based on sequence similarities, a very similar structure was modeled for the class III naphthalene dioxygenase reductase, which transfers electrons to an intermediary ferredoxin, rather than the oxygenase component.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
(c) 2002 Elsevier Science Ltd.
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
318
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
261-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12051836-Acinetobacter, pubmed-meshheading:12051836-Amino Acid Sequence, pubmed-meshheading:12051836-Base Sequence, pubmed-meshheading:12051836-Binding Sites, pubmed-meshheading:12051836-Crystallography, X-Ray, pubmed-meshheading:12051836-Electron Transport, pubmed-meshheading:12051836-Ferredoxin-NADP Reductase, pubmed-meshheading:12051836-Ferredoxins, pubmed-meshheading:12051836-Flavins, pubmed-meshheading:12051836-Iron, pubmed-meshheading:12051836-Models, Molecular, pubmed-meshheading:12051836-Molecular Sequence Data, pubmed-meshheading:12051836-NAD, pubmed-meshheading:12051836-Oxygenases, pubmed-meshheading:12051836-Protein Conformation, pubmed-meshheading:12051836-Protein Structure, Tertiary, pubmed-meshheading:12051836-Sequence Homology, Amino Acid, pubmed-meshheading:12051836-Sulfur
pubmed:year
2002
pubmed:articleTitle
X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1.
pubmed:affiliation
Department of Molecular Biology, Swedish University of Agricultural Sciences, Box 590, BMC, S-751 24 Uppsala, Sweden.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't