Splitting of the O-O bond at the heme-copper catalytic site of respiratory oxidases.

ABSTRACT: Heme-copper oxidases catalyze the four-electron reduction of O₂ to H₂O at a catalytic site that is composed of a heme group, a copper ion (Cu_B), and a tyrosine residue. Results from earlier experimental studies have shown that the O-O bond is cleaved simultaneously with electron transfer from a low-spin heme (heme a/b), forming a ferryl state (P_R ; Fe⁴⁺=O^2-, Cu_B²⁺-OH^-). We show that with the Thermus thermophilus ba₃ oxidase, at low temperature (10°C, pH 7), electron transfer from the low-spin heme b to the catalytic site is faster by a factor of ~10 (τ ≅ 11 μs) than the formation of the P_R ferryl (τ ≅110 μs), which indicates that O₂ is red

SUBMITTER: Poiana F 

PROVIDER: S-EPMC5473675 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature