Linked Life Data

19895641

Source:http://linkedlifedata.com/resource/pubmed/id/19895641

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-12-7
pubmed:abstractText
The qpo gene of Aggregatibacter actinomycetemcomitans encodes a triheme c-containing membrane-bound enzyme, quinol peroxidase (QPO) that catalyzes peroxidation reaction in the respiratory chain and uses quinol as the physiological electron donor. The QPO of A. actinomycetemcomitans is the only characterized QPO, but homologues of the qpo gene are widely distributed among many gram-negative bacteria, including Haemophils ducreii, Bacteroides fragilis, and Escherichia coli. One-third of the amino acid sequence of QPO from the N-terminal end is unique, whereas two-thirds of the sequence from the C-terminal end exhibits high homology with the sequence of the diheme bacterial cytochrome c peroxidase. In order to obtain sufficient protein for biophysical studies, the present study aimed to overproduce recombinant QPO (rQPO) from A. actinomycetemcomitans in E. coli. Coexpression of qpo with E. coli cytochrome c maturation (ccm) genes resulted in the expression of an active QPO with a high yield. Using purified rQPO, we determined the midpoint reduction potentials of the three heme molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1574-6968
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
52-7
pubmed:dateRevised
2010-3-11
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Recombinant expression and redox properties of triheme c membrane-bound quinol peroxidase.
pubmed:affiliation
Department of Microbiology, School of Life Dentistry at Tokyo, The Nippon Dental University, Chiyoda-ku, Tokyo, Japan. eizo.takashima@gmail.com
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't