Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopyReportar como inadecuado




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Bacteria integrate CO2 reduction and acetyl coenzyme-A CoA synthesis in the Wood-Ljungdal pathway. The acetyl-CoA synthase ACS active site is a 4Fe4S-NiNi complex A-cluster. The dinickel site structure with proximal, p, and distal, d, ions was studied by X-ray absorption spectroscopy in ACS variants comprising all three protein domains or only the C-terminal domain with the A-cluster. Both variants showed two square-planar NiII sites and an OH- bound at NiIIp in oxidized enzyme and a H2O at NiIp in reduced enzyme; a NiIp-CO species was induced by CO incubation and a NiII-CH3- species with an additional water ligand by a methyl group donor. These findings render a direct effect of the N-terminal and middle domains on the A-cluster structure unlikely.



Autor: Peer Schrapers, Julia Ilina, Christina M. Gregg, Stefan Mebs, Jae-Hun Jeoung, Holger Dau, Holger Dobbek, Michael Haumann

Fuente: http://plos.srce.hr/



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