Singlet molecular oxygen, O(2)(a(1)Δ(g)), is an intermediate in a variety of processes pertinent to the function of biological systems, including events that result in cell death. Many of these processes involve a reaction between singlet oxygen and a given protein. It is acknowledged that the behavior of a protein can change upon reaction with singlet oxygen, as a result of a structural alteration and/or a direct chemical modification of an active site. However, the converse, where one considers how the behavior of singlet oxygen can be altered by changes in protein structure, has received little attention. In this report, we use a variety of proteins to demonstrate how the rate constant for singlet oxygen removal by a protein responds to (a) protein denaturation, (b) macromolecular crowding of the protein, (c) ligand binding by the protein, and (d) polymerization of the protein. From one perspective, the data show that the kinetics of singlet oxygen removal can be used to monitor protein dynamics. Most importantly, however, the data indicate that protein structural changes that either reveal or cloak a given amino acid residue can have a measurable effect on the overall rate constant for singlet oxygen removal which, in turn, can have ramifications for singlet-oxygen-mediated intracellular events that perturb cell function.
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