Identifying the proton loading site cluster in the ba3 cytochrome c oxidase that loads and traps protons

Biochimica Et Biophysica Acta. Bioenergetics
Xiuhong CaiM R Gunner

Abstract

Cytochrome c Oxidase (CcO) is the terminal electron acceptor in aerobic respiratory chain, reducing O2 to water. The released free energy is stored by pumping protons through the protein, maintaining the transmembrane electrochemical gradient. Protons are held transiently in a proton loading site (PLS) that binds and releases protons driven by the electron transfer reaction cycle. Multi-Conformation Continuum Electrostatics (MCCE) was applied to crystal structures and Molecular Dynamics snapshots of the B-type Thermus thermophilus CcO. Six residues are identified as the PLS, binding and releasing protons as the charges on heme b and the binuclear center are changed: the heme a3 propionic acids, Asp287, Asp372, His376 and Glu126B. The unloaded state has one proton and the loaded state two protons on these six residues. Different input structures, modifying the PLS conformation, show different proton distributions and result in different proton pumping behaviors. One loaded and one unloaded protonation states have the loaded/unloaded states close in energy so the PLS binds and releases a proton through the reaction cycle. The alternative proton distributions have state energies too far apart to be shifted by the electron transfer...Continue Reading

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Citations

May 23, 2021·Biochimica Et Biophysica Acta. Bioenergetics·Sergey A SiletskyMårten Wikström
Jul 3, 2021·Frontiers in Chemistry·Divya KaurM R Gunner
Aug 25, 2021·The Journal of Physical Chemistry. B·Jovan DrageljErnst Walter Knapp

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