Functional Differentiation and Regulatory Mechanisms of Ferrochelatases HemH1 and HemH2 in <i>Bacillus thuringiensis</i> Under Iron and Oxidative Stress.

ABSTRACT: Ferrochelatase is the terminal enzyme in heme biosynthesis. Bacillus thuringiensis (Bt) 97-27 contains two ferrochelatases, HemH1 and HemH2, but their regulatory mechanisms and functional differences under virous environmental stimuli remain unclear. This study confirmed that the iron uptake regulator protein (Fur) bound to the promoters of hemH1 and hemH2, with Fe²⁺ or Fe³⁺ enhancing this binding. Heterologous expression of HemH1 and HemH2 in Escherichia coli showed that pEH2/BL grew better than pEH1/BL under different 2,2'-Bipyridyl, Fe²⁺, and Fe³⁺ concentrations. Under iron limitation, the heme precursor ALA production decreased significantly in both strains. The heme production of pEH2/BL decreased sharply under ir

SUBMITTER: Wang J 

PROVIDER: S-EPMC11988928 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature