Inna Rozman Grinberg

The paper tests the conservation requirements of NrdR binding site basepairs using synthetic DNA fragments and assesses binding affinity of NrdR proteins from different bacteria.

This study characterizes the structure and nucleotide-dependent binding mechanism of E. coli NrdR, revealing its flexibility in adapting to different promoter configurations.

The paper investigates NrdR repressor DNA binding preferences across species, finding optimal spacer lengths between NrdR boxes for efficient binding.

This paper demonstrates that a fused glutaredoxin domain in F. ignava NrdB functions as a reductant for RNR via both dithiol and monothiol mechanisms, and shows the ATP-cone's role in regulating enzyme activity through dATP binding.

The paper identifies an ATP-cone in the radical-generating subunit of RNRs, showing it regulates enzyme activity through quaternary structure changes and dATP-induced tetramer formation.