Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 431, Issue 22, Pages 4514-4522Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2019.08.018
Keywords
Lipoyl synthase; Iron-sulfur proteins; Enzyme mechanism; Electron transfer; Metallo enzyme
Categories
Funding
- COST (European Co-operation in Science and Technology) [CA15133]
- Fondazione Cassa di Risparmio di Firenze [CRF20160985]
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Iron-sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that H-1 NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. H-1 NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. (C) 2019 Elsevier Ltd. All rights reserved.
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