Abstract
DFT calculations were performed for the A-cluster from the enzyme Acetyl-CoA synthase (ACS). The acid constants (pKa), reduction potentials, and pH-dependent reduction potential for the A-cluster with different oxidation states and ligands were calculated. Good agreement of the reduction potentials, dependent on pH in the experiment, was obtained. On the basis of the calculations, a mechanism for the methylation reaction involving two–electron reduction and protonation on the proximal nickel atom of the reduced A-cluster is proposed.
Highlights
CO is formed from the CO2 reduction reaction catalyzed by the carbon monoxide dehydrogenase (CODH) enzyme, and the methyl group is derived from the corrinoid iron-sulfur protein (CoFeSP)
It was shown that only the enzyme with nickel in this site is catalytically active [105]
The energetics of the two-electron reducted A-cluster in the mechanistic steps of catalytical reaction is more favorable than the one-electron reducted one (Section 3.2)
Summary
Acetyl-CoA synthase (ACS) is a bacterial enzyme [1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22] which synthetizes acetylCoA (acetyl coenzyme A) from CO and the methyl group. Several forms of the A–cluster relevant to the catalytic reaction were characterized structurally or spectroscopically [8,36,37,46,56,57,58,59,60,61,62,63,64,65].
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