Steffen Brünle

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 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.

This study uses time-resolved crystallography and MD simulations to reveal structural changes in C1C2 channelrhodopsin during activation, showing how conformational shifts enable ion conduction.

The paper captures the release of a photopharmacological drug from tubulin using time-resolved serial crystallography and shows how ligand release triggers conformational changes.