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The transient complex of poplar plastocyanin with cytochrome f: effects of ionic strength and pH.

Identifieur interne : 003F03 ( Main/Exploration ); précédent : 003F02; suivant : 003F04

The transient complex of poplar plastocyanin with cytochrome f: effects of ionic strength and pH.

Auteurs : Christian Lange [Pays-Bas] ; Tobias Cornvik ; Irene Díaz-Moreno ; Marcellus Ubbink

Source :

RBID : pubmed:15863096

Descripteurs français

English descriptors

Abstract

The orientation of poplar plastocyanin in the complex with turnip cytochrome f has been determined by rigid-body calculations using restraints from paramagnetic NMR measurements. The results show that poplar plastocyanin interacts with cytochrome f with the hydrophobic patch of plastocyanin close to the heme region on cytochrome f and via electrostatic interactions between the charged patches on both proteins. Plastocyanin is tilted relative to the orientation reported for spinach plastocyanin, resulting in a longer distance between iron and copper (13.9 A). With increasing ionic strength, from 0.01 to 0.11 M, all observed chemical-shift changes decrease uniformly, supporting the idea that electrostatic forces contribute to complex formation. There is no indication for a rearrangement of the transient complex in this ionic strength range, contrary to what had been proposed earlier on the basis of kinetic data. By decreasing the pH from pH 7.7 to pH 5.5, the complex is destabilized. This may be attributed to the protonation of the conserved acidic patches or the copper ligand His87 in poplar plastocyanin, which are shown to have similar pK(a) values. The results are interpreted in a two-step model for complex formation.

DOI: 10.1016/j.bbabio.2004.12.002
PubMed: 15863096


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Le document en format XML

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<term>Cytochromes f (chemistry)</term>
<term>Cytochromes f (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term>
<term>Osmolar Concentration (MeSH)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (metabolism)</term>
<term>Plastocyanin (chemistry)</term>
<term>Plastocyanin (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Time Factors (MeSH)</term>
<term>Trees (MeSH)</term>
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<term>Arbres (MeSH)</term>
<term>Brassica napus (MeSH)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Concentration osmolaire (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cytochromes f (composition chimique)</term>
<term>Cytochromes f (métabolisme)</term>
<term>Facteurs temps (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Plastocyanine (composition chimique)</term>
<term>Plastocyanine (métabolisme)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Résonance magnétique nucléaire biomoléculaire (MeSH)</term>
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<term>Plastocyanin</term>
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<term>Plant Proteins</term>
<term>Plastocyanin</term>
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<term>Cytochromes f</term>
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<term>Protéines végétales</term>
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<term>Protein Conformation</term>
<term>Time Factors</term>
<term>Trees</term>
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<term>Concentration osmolaire</term>
<term>Conformation des protéines</term>
<term>Facteurs temps</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Résonance magnétique nucléaire biomoléculaire</term>
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<front>
<div type="abstract" xml:lang="en">The orientation of poplar plastocyanin in the complex with turnip cytochrome f has been determined by rigid-body calculations using restraints from paramagnetic NMR measurements. The results show that poplar plastocyanin interacts with cytochrome f with the hydrophobic patch of plastocyanin close to the heme region on cytochrome f and via electrostatic interactions between the charged patches on both proteins. Plastocyanin is tilted relative to the orientation reported for spinach plastocyanin, resulting in a longer distance between iron and copper (13.9 A). With increasing ionic strength, from 0.01 to 0.11 M, all observed chemical-shift changes decrease uniformly, supporting the idea that electrostatic forces contribute to complex formation. There is no indication for a rearrangement of the transient complex in this ionic strength range, contrary to what had been proposed earlier on the basis of kinetic data. By decreasing the pH from pH 7.7 to pH 5.5, the complex is destabilized. This may be attributed to the protonation of the conserved acidic patches or the copper ligand His87 in poplar plastocyanin, which are shown to have similar pK(a) values. The results are interpreted in a two-step model for complex formation.</div>
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<AbstractText>The orientation of poplar plastocyanin in the complex with turnip cytochrome f has been determined by rigid-body calculations using restraints from paramagnetic NMR measurements. The results show that poplar plastocyanin interacts with cytochrome f with the hydrophobic patch of plastocyanin close to the heme region on cytochrome f and via electrostatic interactions between the charged patches on both proteins. Plastocyanin is tilted relative to the orientation reported for spinach plastocyanin, resulting in a longer distance between iron and copper (13.9 A). With increasing ionic strength, from 0.01 to 0.11 M, all observed chemical-shift changes decrease uniformly, supporting the idea that electrostatic forces contribute to complex formation. There is no indication for a rearrangement of the transient complex in this ionic strength range, contrary to what had been proposed earlier on the basis of kinetic data. By decreasing the pH from pH 7.7 to pH 5.5, the complex is destabilized. This may be attributed to the protonation of the conserved acidic patches or the copper ligand His87 in poplar plastocyanin, which are shown to have similar pK(a) values. The results are interpreted in a two-step model for complex formation.</AbstractText>
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