Document Detail


Intramolecular electron transfer between tryptophan radical and tyrosine in oligoproline-bridged model peptides and hen egg-white lysozyme.
MedLine Citation:
PMID:  9584844     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Long range electron transfer (LRET) across protein matrix underlies all one-electron cellular redox reactions. Elucidation of molecular electron transfer pathways and parametrization of their relative efficiency is one of the most challenging problems in the studies on LRET in proteins. In this paper results of pulse radiolysis investigations on kinetics of LRET accompanying intramolecular radical transformation Trp. --> TyrO. in model peptides built of tryptophan and tyrosine bridged by an oligoproline fragment are reviewed, along with an interpretation of the observed distance dependence of the rate of LRET in terms of conformational properties of the peptides, and partitioning of LRET between electron transfer pathways through space and through peptide backbone. This review on model peptide systems is supplemented with recapitulation of similar studies on the same intramolecular transformation in hen egg-white lysozyme, which allowed to identify Trp./Tyr redox pairs and associated electron transfer pathways involved in LRET in this protein.
Authors:
K L Wierzchowski
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Publication Detail:
Type:  In Vitro; Journal Article; Review    
Journal Detail:
Title:  Acta biochimica Polonica     Volume:  44     ISSN:  0001-527X     ISO Abbreviation:  Acta Biochim. Pol.     Publication Date:  1997  
Date Detail:
Created Date:  1998-07-22     Completed Date:  1998-07-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  14520300R     Medline TA:  Acta Biochim Pol     Country:  POLAND    
Other Details:
Languages:  eng     Pagination:  627-44     Citation Subset:  IM    
Affiliation:
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw. klw@ibbrain.ibb.waw.pl
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MeSH Terms
Descriptor/Qualifier:
Animals
Chickens
Electron Transport*
Female
Free Radicals
Models, Molecular
Muramidase / chemistry,  metabolism
Peptides / chemistry,  metabolism
Proline / chemistry,  metabolism
Protein Conformation
Thermodynamics
Tryptophan / chemistry,  metabolism*
Tyrosine / chemistry,  metabolism*
Chemical
Reg. No./Substance:
0/Free Radicals; 0/Peptides; 147-85-3/Proline; 55520-40-6/Tyrosine; 73-22-3/Tryptophan; EC 3.2.1.17/Muramidase
Comments/Corrections
Erratum In:
Acta Biochim Pol 1998;45(1):288

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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