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Significance Cytochromec oxidase is an important proton pump that utilizes the chemical energy released by oxygen reduction to generate the transmembrane proton concentration gradient. A conserved glutamate residue has been proposed to play a key role in proton pumping, although factors that control the timing and destination of proton transfers by this residue remain poorly understood. By integrating results from multiple computational methodologies, we propose a mechanism in which changes in local hydration and electrostatic interactions regulate the proton affinity of this key residue and, as a result, proton transfer activities. The results highlight the functional significance of local protein motions and hydration state of internal cavities.

Changing hydration level in an internal cavity modulates the proton affinity of a key glutamate in cytochrome c oxidase