Decay of the transient CuB-CO complex is accompanied by formation of the heme Fe-CO complex of cytochrome cbb3-CO at ambient temperature: Evidence from time-resolved fourier transform infrared spectroscopy
SourceJournal of the American Chemical Society
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Time-resolved step-scan Fourier infrared spectroscopy has been used to study the CO-bound cbb3-type cytochrome c oxidase from Pseudomonas stutzeri at room temperature. We observe a single band in the FTIR spectrum at 1956 cm-1 (β-form). The time-resolved data indicate that upon photolysis, CO is transferred from heme b3 (vCO = 1956 cm-1) to CuB (vCO = 2064 cm-1). The decay of the 2065 cm-1 peak (t1/2 = 120 ± 16 ms) and the development of the 1956 cm-1 peak (t1/2 = 144 ± 8 ms ) suggest that formation of the Fe-CO complex is concurrent with the decay of the CuB-CO complex. The intensity ratio of the Fe-CO/CuB-CO (2.15) remains constant for all data points, and thus we conclude that no fraction of CO escapes the binuclear center at 293 K. Copyright © 2002 American Chemical Society.
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