TY - JOUR
T1 - Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba3-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study
AU - Koutsoupakis, Constantinos
AU - Soulimane, Tewfik
AU - Varotsis, Constantinos
PY - 2012/10/26
Y1 - 2012/10/26
N2 - Background: Cytochrome c oxidase reduces O2 to H2O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba3-CO does not lead to a heme a33+-CuB 1+-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a3 and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba3 oxidase are presented.
AB - Background: Cytochrome c oxidase reduces O2 to H2O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba3-CO does not lead to a heme a33+-CuB 1+-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a3 and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba3 oxidase are presented.
UR - http://www.scopus.com/inward/record.url?scp=84868225731&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.403600
DO - 10.1074/jbc.M112.403600
M3 - Article
C2 - 22927441
AN - SCOPUS:84868225731
SN - 0021-9258
VL - 287
SP - 37495
EP - 37507
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 44
ER -