Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5 Suppl
pubmed:dateCreated
1999-12-3
pubmed:abstractText
Mutation of arginine (Arg) 143 with Ile in the monomeric mutant (Phe50Glu, Gly51Glu, Vall48Lys, Ile151Lys) of copper-zinc superoxide dismutase (R143I M4SOD, where M4SOD is the above mutant) leads to a protein with low copper content. Cobalt(II) binds the demetalized protein with a low and comparable affinity for the two metal sites, whereas it binds first and stochiometrically at the zinc site in the M4SOD protein and in the dimeric wild type SOD. However, a CuCo SOD derivative can be obtained whose NMR spectra indicate the structural changes induced by monomerization plus those induced by the Arg ---> Ile mutation. The electronic, circular dichroism, and EPR spectra provide structural information on the copper site. The low activity of the enzyme is accounted for on the basis of the structural properties of the active cavity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1075-4261
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S33-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Structural and functional studies of monomeric mutant of Cu-Zn superoxide dismutase without Arg 143.
pubmed:affiliation
Department of Chemistry and Centro Riosonanze Magnetiche, University of Florence, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't