dc.contributor.author | Pavlou, A. | en |
dc.contributor.author | Soulimane, T. | en |
dc.contributor.author | Pinakoulaki, Eftychia | en |
dc.creator | Pavlou, A. | en |
dc.creator | Soulimane, T. | en |
dc.creator | Pinakoulaki, Eftychia | en |
dc.date.accessioned | 2019-11-21T06:22:12Z | |
dc.date.available | 2019-11-21T06:22:12Z | |
dc.date.issued | 2011 | |
dc.identifier.issn | 1520-6106 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/56002 | |
dc.description.abstract | Resonance Raman (RR) and "light" minus "dark" Fourier transform infrared (FTIR) difference spectra are reported for the CO-bound caa3 oxidase from Thermus thermophilus. Two Fe-CO stretching modes at 518 and 507 cm-1, the Fe-C-O bending mode at 570 cm-1, and three C-O modes of heme a3 at 1958, 1967, and 1973 cm -1 have been identified in the RR and FTIR spectra, respectively. The FTIR "light" minus "dark" spectrum indicates the formation of CuBCO as revealed by its ν(CO) at 2060/2065 cm-1. We assign the bands at 518 (νFe-CO) and 1967/1973 cm-1 (νC-O) as the α-conformation. We also assign the bands at 507 and 1958 cm-1 (νC-O) as originating from the β-conformation of the enzyme. A frequency upshift of the heme a3 Fe-His mode is observed subsequent to CO photolysis from 209 cm-1 in the equilibrium deoxy enzyme to 214 cm-1 in the photoproduct. The caa3 data, distinctly different from those of ba3 oxidase, are discussed in terms of the coupling of the α- and β-conformations that occur in heme-copper oxidases with catalytic function. The dynamics between the heme a3 and heme a propionates as revealed by the perturbation of the bending vibrations δprop of hemes a and a3 at 385 and 392 cm-1, respectively, induced upon CO binding to heme a3 is discussed in terms of the protonic connectivity between the heme a ring-D propionate/Arg site with that of the heme a 3 ring-D propionate-H2O site that leads to the highly conserved in the heme-copper oxidases water pool. © 2011 American Chemical Society. | en |
dc.source | Journal of Physical Chemistry B | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-80053389266&doi=10.1021%2fjp2033356&partnerID=40&md5=389238e11a9762ef4f1e9e398ca614ec | |
dc.subject | Lakes | en |
dc.subject | Vibrations (mechanical) | en |
dc.subject | Catalysis | en |
dc.subject | Copper | en |
dc.subject | FTIR | en |
dc.subject | Photolysis | en |
dc.subject | Enzymes | en |
dc.subject | Conformations | en |
dc.subject | FT-IR spectrum | en |
dc.subject | Fourier transforms | en |
dc.subject | Resonance Raman | en |
dc.subject | Fourier transform infrared | en |
dc.subject | Thermus thermophilus | en |
dc.subject | Porphyrins | en |
dc.subject | Bending modes | en |
dc.subject | Bending vibrations | en |
dc.subject | Catalytic functions | en |
dc.subject | Heme-copper oxidase | en |
dc.subject | Photoproducts | en |
dc.subject | Protonic | en |
dc.subject | Stretching modes | en |
dc.subject | Water pools | en |
dc.title | Evidence for the presence of two conformations of the heme a 3-CuB pocket of cytochrome caa 3 from Thermus thermophilus | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1021/jp2033356 | |
dc.description.volume | 115 | |
dc.description.issue | 39 | |
dc.description.startingpage | 11455 | |
dc.description.endingpage | 11461 | |
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 :5</p> | en |
dc.source.abbreviation | J Phys Chem B | en |
dc.contributor.orcid | Pinakoulaki, Eftychia [0000-0003-3320-6112] | |
dc.gnosis.orcid | 0000-0003-3320-6112 | |