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https://hdl.handle.net/20.500.14279/2030
Title: | Probing the environment of Cu B in heme-copper oxidases | Authors: | Pinakoulaki, Eftychia Varotsis, Constantinos Daskalakis, Vangelis Pinakoulaki, Eftychia |
metadata.dc.contributor.other: | Πινακουλάκη, Ευτυχία Βαρώτσης, Κωνσταντίνος Δασκαλάκης, Ευάγγελος |
Major Field of Science: | Engineering and Technology | Keywords: | Copper compounds;Fourier transform infrared spectroscopy;Ligands;Structural dynamics;Copper;Heme;Chemistry;Enzymology;Infrared spectroscopy | Issue Date: | 14-Aug-2007 | Source: | Journal of physical chemistry B, 2007, vol. 111, no. 35, pp. 10502–10509. | Volume: | 111 | Issue: | 35 | Start page: | 10502 | End page: | 10509 | Journal: | The Journal of Physical Chemistry B | Abstract: | Time-resolved step-scan FTIR (TRS 2-FTIR) and density functional theory have been applied to probe the structural dynamics of Cu B in heme-copper oxidases at room temperature. The TRS 2-FTIR data of cbb 3 from Pseudomonas stutzen indicate a small variation in the frequency of the transient CO bound to Cu B in the pH/pD 7-9 range. This observation in conjunction with density functional theory calculations, in which significant frequency shifts of the v(CO) are observed upon deprotonation and/or detachment of the Cu B ligands, demonstrates that the properties of the CU B ligands including the cross-linked tyrosine, in contrast to previous reports, remain unchanged in the pH 7-9 range. We attribute the small variations in the v(CO) of CUB to protein conformational changes in the vicinity of Cu B. Consequently, the split of the heme Fe-CO vibrations (a-, β-, and γ-forms) is not due to changes in the ligation and/or protonation states of the Cu B ligands or to the presence of one or more ionizable groups, as previously suggested, but the result of global protein conformational changes in the vicinity of Cu B which, in turn, affect the position of Cu B with respect to the heme Fe | URI: | https://hdl.handle.net/20.500.14279/2030 | ISSN: | 15206106 | DOI: | 10.1021/jp0718597 | Rights: | © American Chemical Society | Type: | Article | Affiliation: | University of Crete | Affiliation : | University of Crete | Publication Type: | Peer Reviewed |
Appears in Collections: | Άρθρα/Articles |
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