The three-spin intermediate at the O–O cleavage and proton-pumping junction in heme–Cu oxidases

Abstract

Breaking down oxygen Molecular oxygen (O 2 ) is the terminal oxidant for respiration in mitochondria and many bacteria. Within membrane-bound heme–copper oxidases, a controlled, four-electron reduction of O 2 to water is coupled to pumping of protons across the membrane that can be used, among other outcomes, to generate adenosine triphosphate. Studying cytochrome bo 3 ubiquinol oxidase, Jose et al . investigated the key P M intermediate, which forms after O–O bond cleavage and precedes proton pumping, using magnetic circular dichroism spectroscopy. The authors observed features demonstrating that P M is a three-spin system, which is consistent with a consensus model including an iron(IV)-oxo species, copper(II) ion, and tyrosyl radical. These results provide an important validation of the O–O cleavage mechanism and open the door to understanding the proton pumping step. —MAF