The Fe and Zn cofactor dilemma.

Jiahua Chen, Logan A Calderone, Luying Pan, Trent Quist, Maria-Eirini Pandelia

Journal: Biochimica et biophysica acta. Proteins and proteomics 2023;1871(5):140931

PMID: 37353133

Full Text on Elsevier Science View on PubMed

Abstract

Fe and Zn ions are essential enzymatic cofactors across all domains of life. Fe is an electron donor/acceptor in redox enzymes, while Zn is typically a structural element or catalytic component in hydrolases. Interestingly, the presence of Zn in oxidoreductases and Fe in hydrolases challenge this apparent functional dichotomy. In hydrolases, Fe either substitutes for Zn or specifically catalyzes certain reactions. On the other hand, Zn can replace divalent Fe and substitute for more complex Fe assemblies, known as Fe-S clusters. Although many zinc-binding proteins interchangeably harbor Zn and Fe-S clusters, these cofactors are only sometimes functional proxies.

Address: Department of Biochemistry, Brandeis University, Waltham, MA 02453, USA.; Department of Biochemistry, Brandeis University, Waltham, MA 02453, USA. Electronic address: [email protected].

DOI: 10.1016/j.bbapap.2023.140931

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MeSH Terms: Oxidoreductases, Coenzymes, Oxidation-Reduction, Hydrolases, Zinc