Linked Life Data

8080276

Source:http://linkedlifedata.com/resource/pubmed/id/8080276

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-9-30
pubmed:abstractText
Propionibacterium shermanii contains a single constitutive superoxide dismutase (SOD) which is active with either iron or manganese incorporated in the same protein moiety. Copper and cobalt can also be incorporated by the bacteria in the active center of the SOD under conditions of metal deficiency, but in this case the enzyme is enzymatically inactive. In contrast to other bacterial SODs, the Fe-SOD of P. shermanii remains highly resistant to inactivation by hydrogen peroxide, as does Mn-SOD. Both SOD types cannot be distinguished by their inactivation patterns. Incubation with hydrogen peroxide results in a concentration- and time-dependent decrease in tryptophan fluorescence, independent of the metal present in the active center. Moreover, the Fe-SOD shows a time-dependent decrease in spin concentration after addition of hydrogen peroxide, which reflects alterations in the environment of the metal rather than a reduction of Fe3+ to Fe2+. No obvious correlations exist, however, between these effects and the enzymatic activity of the enzyme. The resistance of the SODs from P. shermanii to inactivation by hydrogen peroxide seems to be caused by the fact that a tryptophan residue near the metal-chelating histidine-75--which is present in all Fe-SODs being rapidly inactivated by this agent--is exchanged for valine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
313
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
296-303
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Reactions of hydrogen peroxide with superoxide dismutase from Propionibacterium shermanii--an enzyme which is equally active with iron or manganese--are independent of the prosthetic metal.
pubmed:affiliation
Chemisches Institut, Tierärztliche Hochschule Hannover, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't