Linked Life Data

2836417

Source:http://linkedlifedata.com/resource/pubmed/id/2836417

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1988-7-13
pubmed:abstractText
During the interconversion of the various cluster types observed in aconitase ([4Fe-4S]1+,2+, [3Fe-4S]0,1+, cubane, or linear types) and production of apoenzyme, changes int he state of the sulfur ligands (RSH and S2-) are bound to occur. We have attempted to obtain information on such changes by interception of SH groups and/or by analysis of the resulting cluster or apoprotein for various forms of sulfur and enzymatic activity. During cluster interconversions no evidence was obtained for changes in SH titer that could be associated with cluster ligands. We conclude from this that the ligand exchange at the cluster is too rapid to allow trapping even by SH reagents of low Mr. The possibility that released SH becomes buried in the protein structure and unreactive cannot be entirely discounted. On formation of the apoenzyme by oxidation with ferricyanide, four SH groups per molecule became unavailable for reaction with 5,5'-dithiobis(2-nitrobenzoic acid); instead, while the holoenzyme contains no disulfides or S(0), two di- or polysulfides were found in the apoenzyme indicating that, on an average, four SH groups and three of the original four S(2-) ligands are trapped as RS-Sx-SR. In agreement with this conclusion is the fact that the apoenzyme can be reconstituted without addition of S(2-). A convenient preparative procedure for reconstitutable apoenzyme in 75% yield is [3Fe-4S] and [4Fe-4S] clusters with a variety of combinations of iron and sulfur isotopes as required for Mössbauer, resonance Raman, and electron nuclear double resonance studies.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8194-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
The state of cluster SH and S2- of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme.
pubmed:affiliation
Department of Biochemistry, Medical College of Wisconsin, Milwaukee 53226.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't