Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2009-3-17
pubmed:abstractText
The resonance Raman (RR) spectra of the oxidized wild-type Archaeoglobus fuglidus 1Fe-Superoxide reductase (SOR), E12V and E12Q mutants were studied at different pH conditions upon excitation in resonance with the pH-dependent charge transfer transition to the ferric iron. The wild-type SOR from Nanoarchaeum equitans that lacks the highly conserved glutamate residue was investigated as a 'natural variant'. No substantial differences were observed in the RR spectra of the active sites of the A. fulgidus proteins. Based on the component analysis in the metal-ligand stretching region the modes involving the Fe-S(Cys) stretching coordinates have been identified. The frequencies of these modes reflect the electronic properties of the Fe-S bond which are related to the catalytic activity of SORs, including reduction of superoxide and product dissociation. Moreover, hydroxide binding to the E12 mutant proteins was demonstrated at high pH. It was further observed that the ferric active site of all three SORs from A. fulgidus senses the presence of phosphate, which possibly replaces the hydroxide at high pH.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1463-9076
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1809-15
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a 'natural variant'.
pubmed:affiliation
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da Republica 127, 2780-157 Oeiras, Portugal. smilja@itqb.unl.pt
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't