dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.contributor.author | Soulimane, T. | en |
dc.contributor.author | Varotsis, Constantinos | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.creator | Soulimane, T. | en |
dc.creator | Varotsis, Constantinos | en |
dc.date.accessioned | 2019-11-21T06:22:21Z | |
dc.date.available | 2019-11-21T06:22:21Z | |
dc.date.issued | 2002 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/56033 | |
dc.description.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 CuB 1+-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 CuB 1+-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. | en |
dc.source | Journal of Biological Chemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037031913&doi=10.1074%2fjbc.M205568200&partnerID=40&md5=ea2f91b19ea9354abb965d3dc0689b1f | |
dc.subject | article | en |
dc.subject | priority journal | en |
dc.subject | unclassified drug | en |
dc.subject | nonhuman | en |
dc.subject | Escherichia coli | en |
dc.subject | enzyme activity | en |
dc.subject | Frequencies | en |
dc.subject | Temperature | en |
dc.subject | room temperature | en |
dc.subject | Fourier transform infrared spectroscopy | en |
dc.subject | complex formation | en |
dc.subject | infrared spectroscopy | en |
dc.subject | Copper | en |
dc.subject | Biochemistry | en |
dc.subject | molecular dynamics | en |
dc.subject | Bacteria (microorganisms) | en |
dc.subject | Enzymes | en |
dc.subject | Protein Binding | en |
dc.subject | Protein Conformation | en |
dc.subject | Binding Sites | en |
dc.subject | enzyme active site | en |
dc.subject | Light | en |
dc.subject | Dissociation | en |
dc.subject | Spectroscopy, Fourier Transform Infrared | en |
dc.subject | heme | en |
dc.subject | Active sites | en |
dc.subject | Cytochrome c Group | en |
dc.subject | Cytochromes a | en |
dc.subject | Cytochromes a3 | en |
dc.subject | Electron Transport Complex IV | en |
dc.subject | Thermus | en |
dc.subject | Thermus thermophilus | en |
dc.subject | cytochrome c oxidase | en |
dc.subject | oxidoreductase | en |
dc.subject | photodynamics | en |
dc.subject | Asperula | en |
dc.subject | cytochrome caa3 oxidase | en |
dc.title | Fourier transform infrared (FTIR) and step-scan time-resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 oxidase from Thermus thermophilus | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1074/jbc.M205568200 | |
dc.description.volume | 277 | |
dc.description.issue | 36 | |
dc.description.startingpage | 32867 | |
dc.description.endingpage | 32874 | |
dc.author.faculty | 002 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Χημείας / Department of Chemistry | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :30</p> | en |
dc.source.abbreviation | J.Biol.Chem. | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.contributor.orcid | Varotsis, Constantinos [0000-0003-2771-8891] | |
dc.gnosis.orcid | 0000-0003-3320-6112 | |
dc.gnosis.orcid | 0000-0003-2771-8891 | |