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|Title:||Decay of the transient Cu B-CO complex is accompanied by formation of the heme Fe-CO complex of cytochrome cbb 3-CO at ambient temperature: evidence from time-resolved fourier transform infrared spectroscopy||Authors:||Stavrakis, Stavros
Fourier transform infrared spectroscopy
|Issue Date:||2002||Publisher:||ACS Publications||Source:||Journal of the american chemical society, 2002, Volume 124, Issue 15, Pages 3814-3815||Abstract:||Time-resolved step-scan Fourier infrared spectroscopy has been used to study the CO-bound cbb 3-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 b 3 (v CO = 1956 cm -1) to CuB (v CO = 2064 cm -1). The decay of the 2065 cm -1 peak (t 1/2 = 120 ± 16 ms) and the development of the 1956 cm -1 peak (t 1/2 = 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||URI:||http://ktisis.cut.ac.cy/handle/10488/6633||ISSN:||00027863||DOI:||10.1021/ja0169825||Rights:||Copyright © 2002 American Chemical Society|
|Appears in Collections:||Άρθρα/Articles|
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