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Mössbauer and EPR studies of activated aconitase: development of a localized valence state at a subsite of the [4Fe-4S] cluster on binding of citrate.
During activation of aconitase a ferrous ion is incorporated into a [3Fe-4S] cluster to yield a structure with a [4Fe-4S] core. Using 57Fe or 56Fe for activation we have studied with Mössbauer spectroscopy the beef heart enzyme in the presence of citrate. Our studies show that the environment of one...
Bewaard in:
| Hoofdauteurs: | , , , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
1983
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC384106/ https://ncbi.nlm.nih.gov/pubmed/6308639 |
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