Structural analogues of the bimetallic reaction center in acetyl CoA synthase: A Ni - Ni model with bound CO

Rachel C. Linck; Cameron W. Spahn; Thomas Rauchfuss; Scott R. Wilson

doi:10.1021/ja035606c

Structural analogues of the bimetallic reaction center in acetyl CoA synthase: A Ni - Ni model with bound CO

Rachel C. Linck, Cameron W. Spahn, Thomas Rauchfuss, Scott R. Wilson

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Models for the active site of the acetyl CoA synthase (ACS) were synthesized by attachment of Cu⁺ and Ni(0) to nickel diaminodithiolate (S₂N₂) and diamidodithiolate (S₂N₂-) complexes. The Ni-Ni species form stable CO adducts, i.e., [{(CO)₂Ni}{NiS₂N₂-}]^2-, whereas the Cu-NiS₂N₂ and Cu-NiS₂N₂- models do not. These results provide supporting evidence for a biological role for reduced nickel in ACS.

Original language	English (US)
Pages (from-to)	8700-8701
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	125
Issue number	29
DOIs	https://doi.org/10.1021/ja035606c
State	Published - Jul 23 2003

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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title = "Structural analogues of the bimetallic reaction center in acetyl CoA synthase: A Ni - Ni model with bound CO",

abstract = "Models for the active site of the acetyl CoA synthase (ACS) were synthesized by attachment of Cu+ and Ni(0) to nickel diaminodithiolate (S2N2) and diamidodithiolate (S2N2-) complexes. The Ni-Ni species form stable CO adducts, i.e., [{(CO)2Ni}{NiS2N2-}]2-, whereas the Cu-NiS2N2 and Cu-NiS2N2- models do not. These results provide supporting evidence for a biological role for reduced nickel in ACS.",

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AU - Linck, Rachel C.

AU - Spahn, Cameron W.

AU - Rauchfuss, Thomas

AU - Wilson, Scott R.

PY - 2003/7/23

Y1 - 2003/7/23

N2 - Models for the active site of the acetyl CoA synthase (ACS) were synthesized by attachment of Cu+ and Ni(0) to nickel diaminodithiolate (S2N2) and diamidodithiolate (S2N2-) complexes. The Ni-Ni species form stable CO adducts, i.e., [{(CO)2Ni}{NiS2N2-}]2-, whereas the Cu-NiS2N2 and Cu-NiS2N2- models do not. These results provide supporting evidence for a biological role for reduced nickel in ACS.

AB - Models for the active site of the acetyl CoA synthase (ACS) were synthesized by attachment of Cu+ and Ni(0) to nickel diaminodithiolate (S2N2) and diamidodithiolate (S2N2-) complexes. The Ni-Ni species form stable CO adducts, i.e., [{(CO)2Ni}{NiS2N2-}]2-, whereas the Cu-NiS2N2 and Cu-NiS2N2- models do not. These results provide supporting evidence for a biological role for reduced nickel in ACS.

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Structural analogues of the bimetallic reaction center in acetyl CoA synthase: A Ni - Ni model with bound CO

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