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...

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Hlavní autoři: Emptage, M H, Kent, T A, Kennedy, M C, Beinert, H, Münck, E
Médium: Artigo
Jazyk:Inglês
Vydáno: 1983
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC384106/
https://ncbi.nlm.nih.gov/pubmed/6308639
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