Linked Life Data

14691678

Source:http://linkedlifedata.com/resource/pubmed/id/14691678

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-3-1
pubmed:abstractText
The Rhodothermus marinus caa(3 )haem-copper oxygen reductase contains all the residues of the so-called D- and K-proton channels, with the notable exception of the helix VI glutamate residue (Glu278(I) in Paracoccus denitrificans aa(3)), being nevertheless a true oxygen reductase reducing O(2) to water, and an efficient proton pump. Instead, in the same helix, but one turn below, it has a tyrosine residue (Tyr256(I), R. marinus caa(3) numbering), whose hydroxyl group occupies the same spatial position as the carboxylate group of Glu278(I), as deduced by comparative modelling techniques. Therefore, we proposed previously that this tyrosine residue could play an important role in the proton pathway. In this article we further study this hypothesis, by investigating the equilibrium thermodynamics of protonation in R. marinus caa(3), using theoretical methodologies based on the structural model previously obtained. Control calculations are also performed for the P. denitrificans aa(3) oxygen reductase. In both oxygen reductases we find several residues that are proton active (i.e., that display partial protonation) at physiological pH, some of them being redox sensitive (i.e., sensitive to the protein redox state). However, the caa(3 )Tyr256(I) is not proton active at physiological pH, in contrast to the aa(3) Glu278(I) which is both proton active at physiological pH and shows a high redox sensitivity. In R. marinus caa(3) we do not find any other residues in the same protein zone that can have this property. Therefore, there are no putative D-channel residues that are proton active in this oxidase. The protonatable residues of the K-channel are much more functionally conserved in both oxygen reductases than the same type of residues in the D-channel. Two (Tyr262(I) and Lys336(I), caa(3) numbering) out of three protonatable K-channel residues are proton active and redox sensitive in both proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0949-8257
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
124-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase.
pubmed:affiliation
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, Av. da República, 2781-901 Oeiras, Portugal. claudio@itqb.unl.pt
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't