Literature summary for 6.2.1.1 extracted from

Webster, C.E.; Darensbourg, M.Y.; Lindahl, P.A.; Hall, M.B.
Structures and energetics of models for the active site of acetyl-coenzyme A synthase: role of distal and proximal metals in catalysis (2004), J. Am. Chem. Soc., 126, 3410-3411.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Ni	the authors favor a mechanism in which methylation occurs first to Ni(p0 -) or Ni(pI -)[Fe4S4]+, followed by coordination of CO to form Ni(pII)(CO)(CH3) which breaks one of the S(Nid) bonds (forming the bis square planar Ni(II) species, as if the Ni(d)N2S2 unit were acting as a biological pseudodiphosphine, mimicking behavior common to a bidentate phosphine). The CO-insertion/CH3-migration occurs on one metal forming the trigonal planar Ni(pII)-acetyl intermediate. Finally, addition of thiolate produces the thioester. The authors disfavor the unprecedented bimetallic, CO-insertion/CH3-migration mechanism (both in its diamagnetic and paramagnetic guise) and disfavors CO, CH3+, or thiolate (CoA) binding to the distal Ni. Finally, Ni in the proximal site produces a better catalyst than does Cu	Moorella thermoacetica

Organism

Organism	UniProt	Comment	Textmining
Moorella thermoacetica	-	-	-

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Release 2023.1 (January 2023)