Comparative Dynamics Enables Discovery of Embedded Bacterial Ferredoxin Domains in Large Redox Enzymes.

ABSTRACT: Bacterial ferredoxins are small iron-sulfur binding proteins that function as soluble electron shuttles between redox enzymes in the cell. Their simple 2×(β-α-β) fold, central metabolic function, and ubiquity across all kingdoms of life have led to the proposal that ferredoxins were likely among the earliest proteins. Today, ferredoxin-like folds are embedded in large, multidomain enzymes, suggesting ancient gene duplication and fusion events. In some cases, these embedded domains may have scant sequence or even structural homology to soluble counterparts, challenging the use of traditional phylogenetic tools to establish evolutionary relationships. In this study, we identify fragments of bacterial ferredoxins within larger oxidoreductases by integrating comparative sequence, structure, an

SUBMITTER: Siess JA 

PROVIDER: S-EPMC12517254 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature