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Evidence for lanthanide and PQQ dependent dehydrogenases in Eukarya

2026/07/14 by Colin Michael Robinson, Norma Cecilia Martinez-Gomez, Jacob A West-Roberts +2 · 1 voice
Biochemistry, Genetics and Molecular Biology · Energy · #Metalloenzymes and iron-sulfur proteins #Microbial Metabolic Engineering and Bioproduction #Microbial metabolism and enzyme function

paper · pdf · doi:10.64898/2026.07.14.738520

openalex publication_date 2026/07/14 · openalex created_date 2026/07/16 · openalex updated_date 2026/07/22

Abstract

Abstract Lanthanides function as enzyme cofactors in bacteria, where they are widely distributed in pyrroloquinoline quinone-dependent 8-bladed beta-propeller dehydrogenases. No lanthanide-dependent enzymes, however, have been described outside prokaryotes. Here, we combined structural bioinformatics, phylogenetics, AlphaFold3 co-folding, coordination-sphere comparison, and quantum-mechanical cluster modeling to search for and rank putative lanthanide-coordinating 8-bladed beta-propeller enzymes in Eukarya. We identified candidate lanthanide-coordinating proteins in a diverse range of eukaryotes, predominantly plants and fungi, including species of clear industrial and agricultural relevance. A high-confidence subset matched validated bacterial Ln-binders based on both geometric similarity to canonical Ln-binding sites and on predicted Ln 3+ versus Ca 2+ selectivity. Our findings indicate that lanthanide biology likely extends beyond bacteria, with implications for plant, fungal, and broader eukaryotic metabolism, and warrant targeted biochemical investigation.

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