January 1, 2003Chemical Communications

Capture of Ni II , Cu I and Zn II by thiolate sulfurs of an N 2 S 2 Ni complex: A role for a metallothiolate ligand in the acetyl-coenzyme A synthase active site

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Abstract

The metal binding affinity of an (N2S2)Ni bridging metallothiolate ligand (Zn2+ < Ni2+ < Cu+) gives precedent for the observed heterogeneity in ACS/CODH.

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Golden et al. (2003) studied this question.

synapsesocial.com/papers/6aa66674e46a8f60379227eb https://doi.org/10.1039/b304884p

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Abstract

The metal binding affinity of an (N2S2)Ni bridging metallothiolate ligand (Zn2+ < Ni2+ < Cu+) gives precedent for the observed heterogeneity in ACS/CODH.

Capture of Ni II , Cu I and Zn II by thiolate sulfurs of an N 2 S 2 Ni complex: A role for a metallothiolate ligand in the acetyl-coenzyme A synthase active site

Abstract

Discussion

Cite This Study

Capture of Ni II , Cu I and Zn II by thiolate sulfurs of an N 2 S 2 Ni complex: A role for a metallothiolate ligand in the acetyl-coenzyme A synthase active site

Abstract

Discussion

Cite This Study

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