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Titolo:
Structural changes of cytochrome c(552) from Thermus thermophilus adsorbedon anionic and hydrophobic surfaces probed by FTIR and 2D-FTIR spectroscopy
Autore:
Lecomte, S; Hilleriteau, C; Forgerit, JP; Revault, M; Baron, MH; Hildebrandt, P; Soulimane, T;
Indirizzi:
Univ Paris 06, CNRS, UMR 7075, Lab Dynam Interact & React, F-94320 Thiais,France Univ Paris 06 Thiais France F-94320 eract & React, F-94320 Thiais,France Max Planck Inst Strahlenchem, D-45470 Mulheim, Germany Max Planck Inst Strahlenchem Mulheim Germany D-45470 70 Mulheim, Germany Klinikum Aachen, Inst Biochem, D-52057 Aachen, Germany Klinikum Aachen Aachen Germany D-52057 Biochem, D-52057 Aachen, Germany
Titolo Testata:
CHEMBIOCHEM
fascicolo: 3, volume: 2, anno: 2001,
pagine: 180 - 189
SICI:
1439-4227(20010302)2:3<180:SCOCCF>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESONANCE RAMAN-SPECTROSCOPY; ELECTRON-TRANSFER REACTION; C-OXIDASE; PARACOCCUS-DENITRIFICANS; INFRARED-SPECTRA; BINDING; ABSORPTION; MONTMORILLONITE; ADSORPTION; RESOLUTION;
Keywords:
cytochromes; electron transport; heme proteins; IR spectroscopy; protein structures;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Lecomte, S Univ Paris 06, CNRS, UMR 7075, Lab Dynam Interact & React, 2 Rue Henri Dunant, F-94320 Thiais, France Univ Paris 06 2 Rue Henri Dunant Thiais France F-94320 France
Citazione:
S. Lecomte et al., "Structural changes of cytochrome c(552) from Thermus thermophilus adsorbedon anionic and hydrophobic surfaces probed by FTIR and 2D-FTIR spectroscopy", CHEMBIOCHEM, 2(3), 2001, pp. 180-189

Abstract

The structural changes of cytochrome C-552 bound to anionic and hydrophobic clay surfaces have been investigated by Fourier transform infrared spectroscopy. Binding to the anionic surface of montmorillonite is controlled by electrostatic interactions since addition of electrolyte (0.5 mol L-1 KCl) causes desorption of more than 2/3 Of the protein molecules. Electrostatic binding occurs through the back side of the protein (i.e., remote from the heme site) and is associated only with subtle changes of the secondary structure. In contrast, adsorption to the hydrophobic surface of talc leads to a decrease in a-helical structure by ca. 5% and an increase in beta -sheet structure by ca. 6%. These structural changes are attributed to a hydrophobic region on the front surface of cytochrome C-552 close to the partially exposed heme edge. This part on the protein surface is identified as the interaction domain for talc and most likely also serves for binding to the natural reaction partner, a ba(3)-oxidase. Fourier transform infrared spectra of cytochrome c(552) and the clay -cylochrome c(552) complexes have been measured as a function of time following dissolution and suspension in deuterated buffer, respectively. A two-dimensional correlation analysis was applied to these spectra to investigate the dynamics of the structural changes in the protein. For both complexes, adsorption and subsequent unfolding processes in the binding domains are faster than the time resolution of the spectroscopic experiments. Thus, the processes that could be monitored are refolding of peptide segments and side chain rearrangements following the adsorption-induced perturbation of the protein structure and the solvation of the adsorbed protein. In each case, side chain alterations of solvent-exposed tyrosine, aspartate, and glutamate residues were observed. For the cytochrome c(552)-talc complex, these changes are followed by a slow refolding ofthe peptide chain in the binding domain and, subsequently, a further H/D exchange of amide group protons.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 22:51:15