Microbes vary strategically in their metalation of mononuclear enzymes.

ABSTRACT: Studies have determined that nonredox enzymes that are cofactored with Fe(II) are the most oxidant-sensitive targets inside Escherichia coli. These enzymes use Fe(II) cofactors to bind and activate substrates. Because of their solvent exposure, the metal can be accessed and oxidized by reactive oxygen species, thereby inactivating the enzyme. Because these enzymes participate in key physiological processes, the consequences of stress can be severe. Accordingly, when E. coli senses elevated levels of H₂O₂, it induces both a miniferritin and a manganese importer, enabling the replacement of the iron atom in these enzymes with manganese. Manganese does not react with H₂O₂ and thereby preserves enzyme activity. In this study, we examine

SUBMITTER: Rohaun SK 

PROVIDER: S-EPMC11127058 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature