Issue 15, 2004
From the journal:

Chemical Communications

Binding of CO to structural models of the bimetallic subunit at the A-cluster of acetyl coenzyme A synthase/CO dehydrogenase†

Todd C. Harrop,a   Marilyn M. Olmsteadb  and  Pradip K. Mascharak*a  

* Corresponding authors

a Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA

b Department of Chemistry, University of California, Davis, CA 95616, USA

Abstract

Trinuclear Ni–Cu–Ni and Ni–Ni–Ni complexes derived from an Ni(II)–dicarboxamido–dithiolato metallosynthon exhibit redox behavior and CO binding properties similar to those of the A-cluster in acetyl coenzyme A synthase/CO dehydrogenase (ACS/CODH).

Graphical abstract: Binding of CO to structural models of the bimetallic subunit at the A-cluster of acetyl coenzyme A synthase/CO dehydrogenase

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Article information

DOI
https://doi.org/10.1039/B405572C
Article type
Communication
Submitted
14 Apr 2004
Accepted
03 Jun 2004
First published
12 Jul 2004

Chem. Commun., 2004, 1744-1745

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Binding of CO to structural models of the bimetallic subunit at the A-cluster of acetyl coenzyme A synthase/CO dehydrogenase

T. C. Harrop, M. M. Olmstead and P. K. Mascharak, Chem. Commun., 2004, 1744 DOI: 10.1039/B405572C

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