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Title: Fourier transform infrared (FTIR) and step-scan time-resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 oxidase from Thermus thermophilus
Authors: Pinakoulaki, Eftychia 
Soulimane, Tewfik 
Varotsis, Constantinos 
Keywords: Biochemistry;Copper;Enzymes;Fourier transform infrared spectroscopy;Dissociation;Cytochrome oxidase;Heme;Protein binding
Issue Date: 2002
Publisher: American Society for Biochemistry and Molecular Biology
Source: Journal of biological chemistry, 2002, Volume 277, Issue 36, Pages 32867-32874
Abstract: Fourier transform infrared (FTIR) and step-scan time-resolved FTIR difference spectra are reported for the [carbonmonoxy]cytochrome caa3 from Thermus thermophilus. A major C-O mode of heme a3 at 1958 cm-1 and two minor modes at 1967 and 1975 cm-1 (7:1:1) have been identified at room temperature and remained unchanged in H2O/D2O exchange. The observed C-O frequencies are 10 cm-1 higher than those obtained previously at 21 K (Einarsdóttir, O., Killough, P. M., Fee, J. A., and Woodruff, W. H. (1989) J. Biol. Chem. 264, 2405-2408). The time-resolved FTIR data indicate that the transient CuB1+-CO complex is formed at room temperature as revealed by the CO stretching mode at 2062 cm-1. Therefore, the caa3 enzyme is the only documented member of the heme-copper superfamily whose binuclear center consists of an a3-type heme of a β-form and a CuB atom of an α-form. These results illustrate that the properties of the binuclear center in other oxidases resulting in the α-form are not required for enzymatic activity. Dissociation of the transient CuB1+-CO complex is biphasic. The rate of decay is 2.3 x 104 s-1 (fast phase, 35%) and 36.3 s-1 (slow phase, 65%). The observed rate of rebinding to heme a3 is 34.1 s-1. The implications of these results with respect to the molecular motions that are general to the photodynamics of the binuclear center in heme-copper oxidases are discussed
ISSN: 00219258
DOI: 10.1074/jbc.M205568200
Rights: © 2002 by The American Society for Biochemistry and Molecular Biology, Inc
Type: Article
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