Mössbauer studies of beef heart aconitase: evidence for facile interconversions of iron-sulfur clusters.

Beef heart aconitase, isolated under aerobic conditions, has been studied with Mössbauer and EPR spectroscopy. In the oxidized state, the enzyme exhibits an EPR signal at g = 2.01. The Mössbauer data show that this signal is associated with a 3Fe cluster. In dithionite-reduced aconitase, the 3Fe clu...

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Bibliografische gegevens

Gepubliceerd in:	Proc Natl Acad Sci U S A
Hoofdauteurs:	Kent, T A, Dreyer, J L, Kennedy, M C, Huynh, B H, Emptage, M H, Beinert, H, Münck, E
Formaat:	Artigo
Taal:	Inglês
Gepubliceerd in:	National Academy of Sciences 1982
Onderwerpen:	Research Article
Online toegang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC345907/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6280166/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.79.4.1096
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