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Experimental and numerical study of the poplar plastocyanin isoforms using Tyr as a probe for electrostatic similarity and dissimilarity.

Identifieur interne : 004273 ( Main/Exploration ); précédent : 004272; suivant : 004274

Experimental and numerical study of the poplar plastocyanin isoforms using Tyr as a probe for electrostatic similarity and dissimilarity.

Auteurs : A. Shosheva [Bulgarie] ; A. Donchev ; M. Dimitrov ; I. Zlatanov ; G. Toromanov ; V. Getov ; E. Alexov

Source :

RBID : pubmed:15063316

Descripteurs français

English descriptors

Abstract

A detailed study of the tyrosine spectral characteristics was carried out in a broad range of pHs for both isoforms of plastocyanin from poplar. It was found that Tyr 80 is always protonated while Tyr 83 can form a tirosinate at high pHs. The pK(a) of Tyr 83 is practically identical in plastocyanin a and b, but the quenching of its spectrum is different in the isoforms. This provides insights that the acidic patches surrounding Tyr 83 have different electrostatic properties in plastocyanin a and b. The protonation states and the electrostatic interactions were numerically modeled on the existing plastocyanin a structure and on a homology model of plastocyanin b. The results of numerical calculations agree with the experimental findings and identify several differences in the titration behavior of the acidic patches. The difference of the tyrosine quenching pH profiles of the isoforms is rationalized by the differences in the calculated pK(a)'s of amino acids in the neighboring acidic clusters.

DOI: 10.1016/j.bbapap.2003.10.010
PubMed: 15063316


Affiliations:


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Le document en format XML

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<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Molecular Probes (MeSH)</term>
<term>Plastocyanin (chemistry)</term>
<term>Plastocyanin (metabolism)</term>
<term>Populus (chemistry)</term>
<term>Populus (metabolism)</term>
<term>Protein Isoforms (chemistry)</term>
<term>Protein Isoforms (metabolism)</term>
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<term>Acrylamide (métabolisme)</term>
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<term>Concentration en ions d'hydrogène (MeSH)</term>
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<term>Isoformes de protéines (composition chimique)</term>
<term>Isoformes de protéines (métabolisme)</term>
<term>Plastocyanine (composition chimique)</term>
<term>Plastocyanine (métabolisme)</term>
<term>Populus (composition chimique)</term>
<term>Populus (métabolisme)</term>
<term>Sondes moléculaires (MeSH)</term>
<term>Spectrophotométrie (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Tyrosine (MeSH)</term>
<term>Électricité statique (MeSH)</term>
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<term>Plastocyanin</term>
<term>Protein Isoforms</term>
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<term>Plastocyanin</term>
<term>Protein Isoforms</term>
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<div type="abstract" xml:lang="en">A detailed study of the tyrosine spectral characteristics was carried out in a broad range of pHs for both isoforms of plastocyanin from poplar. It was found that Tyr 80 is always protonated while Tyr 83 can form a tirosinate at high pHs. The pK(a) of Tyr 83 is practically identical in plastocyanin a and b, but the quenching of its spectrum is different in the isoforms. This provides insights that the acidic patches surrounding Tyr 83 have different electrostatic properties in plastocyanin a and b. The protonation states and the electrostatic interactions were numerically modeled on the existing plastocyanin a structure and on a homology model of plastocyanin b. The results of numerical calculations agree with the experimental findings and identify several differences in the titration behavior of the acidic patches. The difference of the tyrosine quenching pH profiles of the isoforms is rationalized by the differences in the calculated pK(a)'s of amino acids in the neighboring acidic clusters.</div>
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<AbstractText>A detailed study of the tyrosine spectral characteristics was carried out in a broad range of pHs for both isoforms of plastocyanin from poplar. It was found that Tyr 80 is always protonated while Tyr 83 can form a tirosinate at high pHs. The pK(a) of Tyr 83 is practically identical in plastocyanin a and b, but the quenching of its spectrum is different in the isoforms. This provides insights that the acidic patches surrounding Tyr 83 have different electrostatic properties in plastocyanin a and b. The protonation states and the electrostatic interactions were numerically modeled on the existing plastocyanin a structure and on a homology model of plastocyanin b. The results of numerical calculations agree with the experimental findings and identify several differences in the titration behavior of the acidic patches. The difference of the tyrosine quenching pH profiles of the isoforms is rationalized by the differences in the calculated pK(a)'s of amino acids in the neighboring acidic clusters.</AbstractText>
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