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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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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1989
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC298599/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2557631/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.86.24.9846 |
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