Kanwal Kayastha

The paper presents cryo-EM structures of Escherichia coli cytochrome bd-I to elucidate its mechanism of quinol oxidation and inhibition, identifying key residues and structural changes involved in catalysis and drug binding.

This study reveals how BCRII enzymes use electron-bifurcation modules to reduce aromatic rings beyond typical biological redox limits.

This study investigates the redox regulation of Mycobacterium tuberculosis cytochrome bd by its disulfide bond and quinone specificity, showing reduced activity upon disulfide reduction and substrate inhibition with menaquinol.