Abstract
The reaction of cytochrome-c-oxidase with O2 has been reinvestigated at 2 degrees C by a flow laser pulsed method. The experiments indicate that a new spectral intermediate, populated with a rate constant of approximately 5000/s, is observed in a wavelength range in which heme a is the only chromophore (445 and 430 nm). The results are interpreted with reference to previous data obtained in the near infrared region, and it is suggested that breakage of the (enzyme bound) dioxygen bond is associated to a spectral perturbation of the cytochrome a3-CuB binuclear center.
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Selected References
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