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Literature summary for 1.97.1.4 extracted from

  • Dey, A.; Peng, Y.; Broderick, W.E.; Hedman, B.; Hodgson, K.O.; Broderick, J.B.; Solomon, E.I.
    S K-edge XAS and DFT calculations on SAM dependent pyruvate formate-lyase activating enzyme: nature of interaction between the Fe4S4 cluster and SAM and its role in reactivity (2011), J. Am. Chem. Soc., 133, 18656-18662.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Escherichia coli
[4Fe-4S]-center an increase in pre-edge intensity is due to additional contributions from sulfide and thiolate of the Fe4S4 cluster into the C-S sigma* orbital. There is a backbonding interaction between the Fe4S4 cluster and C-S sigma* orbitals of S-adenosyl-L-methionine in this inner sphere complex. This backbonding is enhanced in the reduced form and this configurational interaction between the donor and acceptor orbitals facilitates the electron transfer from the cluster to S-adenosyl-L-methionine, that otherwise has a large outer sphere electron transfer barrier. The energy of the reductive cleavage of the C-S bond is sensitive to the dielectric of the protein in the immediate vicinity of the site as a high dielectric stabilizes the more charge separated reactant increasing the reaction barrier Escherichia coli