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Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase.

Active beef heart aconitase contains an iron-sulfur cluster with an [Fe4S4]2+ core. This cluster can be converted into Fe3S4 with concomitant loss of enzymatic activity. We have reconstituted apo-aconitase with iron and selenide to obtain Fe4Se4 aconitase. The Se analog has higher catalytic activity...

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Autors principals: Surerus, K K, Kennedy, M C, Beinert, H, Münck, E
Format: Artigo
Idioma:Inglês
Publicat: 1989
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC298599/
https://ncbi.nlm.nih.gov/pubmed/2557631
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