A Nickel Tripeptide as a Metallodithiolate Ligand Anchor for Resin-Bound Organometallics

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Green, Kayla N.; Jeffery, Stephen P.; Reibenspies, Joseph H.; Darensbourg, Marcetta Y.;
(2006)
  • Publisher: Figshare
  • Related identifiers: doi: 10.1021/ja060876r.s002, doi: 10.1021/ja060876r.s001
  • Subject: Molecular Biology | synthesis | Metallodithiolate Ligand Anchor | Biotechnology | organometallic chemistry | support anchor | NiN 2 S 2 metalloligands | heterobimetallic complexes | Reflectance FTIR spectroscopy | nickel atoms | bidentate ligands | Nickel Tripeptide | resin beads | catalyst | Biochemistry | evolutionarily optimized nickel peptide | N 2 S 2 | Biophysics | NiN 2 S 2 portion | acetyl CoA synthase enzyme | CGC
    • FOR: 69999 Biological Sciences not elsewhere classified | 39999 Chemical Sciences not elsewhere classified

The molecular structure of the acetyl CoA synthase enzyme has clarified the role of individual nickel atoms in the dinickel active site which mediates C−C and C−S coupling reactions. The NiN<sub>2</sub>S<sub>2</sub> portion of the biocatalyst (N<sub>2</sub>S<sub>2... View more
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