A protein-based model of carbon monoxide dehydrogenase exhibits tunable covalency across cluster oxidation and ligand-bound states

Chemical Science 2026 Open access

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Authors: Luke C. Lewis, Prajakta Badve, Itzel P Vaca, Pujan Ajmera, Yuri Lee, Anastassia N. Alexandrova, Katlyn K. Meier, Hannah S. Shafaat
DOI: 10.1039/d6sc00023a
Cited by: 3
References: 91

Abstract

A nickel–iron–sulfur cluster model of the CO 2 -fixing enzyme, CODH, has been studied using spectroscopy and computation. The supporting iron–sulfur fragment balances charge and spin from the nickel site across redox states to control reactivity.

Fields of Study & Subjects

Metalloenzymes and iron-sulfur proteins Metal-Catalyzed Oxygenation Mechanisms Photosynthetic Processes and Mechanisms

Publication details

Journal / source
Chemical Science
Publisher
Royal Society of Chemistry (RSC)
Volume
17
Issue
22
Pages
11042–11061
Publication date
1 January 2026
Language
EN