Linked Life Data

12054744

Source:http://linkedlifedata.com/resource/pubmed/id/12054744

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-6-10
pubmed:abstractText
The A-type flavoproteins (ATF) are modular proteins involved in multi-component electron transfer pathways, having oxygen reductase activity. They are complex flavoproteins containing two distinct structural domains, one having an FMN in a flavodoxin-like fold and the other a binuclear iron centre within a metallo-beta-lactamase-like fold. Here, we report the purification and characterisation of a recombinant ATF from the cyanobacterium Synechoystis sp. PCC 6803, which has the unique feature of comprising an additional third domain with similarities towards flavin:NAD(P)H reductases. The latter was expressed independently as a truncated protein form and found to be capable of receiving electrons from NADH as well as to indiscriminately bind either one FAD or one FMN with equivalent affinities. Further kinetic studies have shown that the intact ATF is an NADH:oxygen oxidoreductase, with the catalytic ability to fully reduce oxygen to water. Thus, this constitutes an example on how structural modules found within partner proteins from an electron transfer pathway can be combined in a single polypeptide chain achieving identical catalytic activities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
82-7
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Module fusion in an A-type flavoprotein from the cyanobacterium Synechocystis condenses a multiple-component pathway in a single polypeptide chain.
pubmed:affiliation
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, Apt 127, 2780-156 Oeiras, Portugal.
pubmed:publicationType
Journal Article