Elucidation of the mechanism by which catecholamine stress hormones liberate iron from the innate immune defense proteins transferrin and lactoferrin.

The ability of catecholamine stress hormones and inotropes to stimulate the growth of infectious bacteria is now well established. A major element of the growth induction process has been shown to involve the catecholamines binding to the high-affinity ferric-iron-binding proteins transferrin (Tf) and lactoferrin, which then enables bacterial acquisition of normally inaccessible sequestered host iron. The nature of the mechanism(s) by which the stress hormones perturb iron binding of these key innate immune defense proteins has not been fully elucidated.

Evidence for a novel bisacylphosphine oxide photoreaction from TRIR, TREPR and DFT studies.

Magnetic field effects on the photolysis of homogeneous solutions containing (2,4,6-trimethylbenzoyl)diphenylphoshine oxide, MAPO, and bis(2,4,6-trimethylbenzoyl)phenylphosphine oxide, BAPO, were studied using time-resolved infrared spectroscopy. The two molecules display distinctly different field dependences in conflict with established photochemistry. Time-resolved EPR was employed to examine the photochemistry in detail, resulting in the detection of previously unobserved radical species when BAPO was photoexcited in alcoholic solvents.