The kinetics and thermodynamics of the reaction of solid-state fully reduced membrane-bound cytochrome oxidase with carbon monoxide as studied by dual-wavelength multichannel spectroscopy and flash photolysis.
1. The results of non-linear optimization studies on the mechanism of reaction of solid-state fully reduced membrane-bound cytochrome oxidase with CO over the 178--203 K range are presented. The analysis is carried out on data obtained by dual-wavelength multichannel spectroscopy at three wavelength pairs (444--463 nm, 590--630 nm and 608--630 nm), which yield three distinct progress curves. The only model that satisfies the triple requirement of a standard deviation within the standard error of the data, a random distribution of residuals and good determination of the optimized parameters is a two-species sequential mechanism: flash photolysis yields unliganded cytochrome oxidase and free CO, which then recombine to form species Ic; Ic is then converted into species IIc, which is identical with the cytochrome oxidase-CO complex existing before flash photolysis. All the thermodynamic parameters describing this model are calculated. 2. On the basis of the data obtained from this paper, together with data from potentiometric studies, magnetic susceptibility measurements and i.r. spectroscopy, the chemical identity of the species is suggested.
D001665:Binding Sites; D002248:Carbon Monoxide / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000378:metabolism*; D004789:Enzyme Activation; D007700:Kinetics; D008956:Models, Chemical; D010782:Photolysis; D013057:Spectrum Analysis; D013696:Temperature; D013816:Thermodynamics
D002248:Carbon Monoxide; D003576:Electron Transport Complex IV