Seong Ok Kim

Abstract Iron is an essential cofactor for fundamental biological processes. However, Fe(III) is poorly soluble under aerobic conditions, limiting its bioavailability. To secure this essential nutrient, bacteria release high-affinity siderophores that capture environmental Fe(III) and are subsequently imported into the cell as ferric siderophore complexes.

Abstract The Light-oxygen-voltage-sensing domain (LOV) superfamily, found in enzymes and signal transduction proteins, plays a crucial role in converting light signals into structural signals, mediating various biological mechanisms. While time-resolved spectroscopic studies have revealed the dynamics of the LOV-domain chromophore’s electronic structures, understanding the structural changes in the protein moiety, particularly regarding light-induced dimerization, remains challenging.

Abstract Understanding protein structure and kinetics under physiological conditions is crucial for elucidating complex biological processes. While time-resolved (TR) techniques have advanced to track molecular actions, their practical application in biological reactions is often confined to reversible photoreactions within limited experimental parameters due to inefficient sample utilization and inflexibility of experimental setups.