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• W2477485013 abstract "Cytochrome c oxidase (CcO) has four redox-active metal sites, Fe a , Fe a3 , CuA and CuB. Each site reversibly receives one electron equivalent. The four electron equivalents required to reduce the bound O2 are sequentially transferred from cytochrome c and each is coupled to the pumping of one proton equivalent. The purified enzyme fraction as prepared (the resting oxidized form) is not involved in catalytic turnover since one electron reduction of the resting oxidized form is not coupled to proton pumping. Redox and resonance Raman data suggest that a peroxide molecule bridges Fe a3 and CuB in the O2 reduction site. X-ray structural analyses show that the O-O bond length is 1.7 A, which is significantly longer than that of the typical peroxide bridge between two metals (1.5 A), suggesting an activated state of the bound peroxide. On the other hand, investigation of a bacterial CcO produced the proposal that the bound peroxide is not the intrinsic ligand; instead the peroxide is formed from hydroxyl radicals created by the strong X-ray radiation. Establishment of the ligand structure in the O2 reduction site is a prerequisite for elucidation of the proton-pumping mechanism." @default.
• W2477485013 created "2016-08-23" @default.
• W2477485013 creator A5028432382 @default.
• W2477485013 date "2016-01-01" @default.
• W2477485013 modified "2023-09-22" @default.
• W2477485013 title "XFEL Studies on Bovine Heart Cytochrome c Oxidase" @default.
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• W2477485013 doi "https://doi.org/10.1007/978-94-017-7481-9_18" @default.
• W2477485013 hasPublicationYear "2016" @default.
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