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Article

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

PloS one - 1 Jan 2017

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

Abstract excerpt

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...

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PMID: 28178309
DOI: 10.1371/journal.pone.0171039
PMCID: PMC5298270

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