Document Detail


Studies on the DT-diaphorase-catalysed reaction employing quinones as substrates: evidence for a covalent modification of DT-diaphorase by tetrachloro-p-benzoquinone.
MedLine Citation:
PMID:  14726156     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In this study, the kinetic parameters, V(max) and K(m), of rat liver DT-diaphorase were determined for a series of p-benzoquinones, with methyl, methoxy, cyano, hydroxy and halo substituents. The results show that there is no correlation between the experimentally determined rates of p-benzoquinone reduction by DT-diaphorase and the calculated chemical reactivity of the examined substrates as expressed by the energy of the lowest unoccupied molecular orbital, E(LUMO). However, a reasonable correlation was found between the natural logarithm of V(max)/K(m) and the partition coefficient of the p-benzoquinones (r=0.81). Furthermore, tetrachloro-p-benzoquinone, one of the tested quinones is shown to be an inhibitor of rat DT-diaphorase. The presence of bovine serum albumin (BSA) in the incubation mixture protects DT-diaphorase against the inactivation by tetrachloro-p-benzoquinone, probably by interacting with the quinone. Maldi-Tof analysis of the incubation mixture of the purified DT-diaphorase and tetrachloro-p-benzoquinone showed that every subunit of the enzyme shifted about +414 amu, whereas the dimer shifted about +849 amu relative to control values. This indicates a covalent modification of the rat liver DT-diaphorase by tetrachloro-p-benzoquinone.
Authors:
Ahmed M Osman; Sjef Boeren
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Chemico-biological interactions     Volume:  147     ISSN:  0009-2797     ISO Abbreviation:  Chem. Biol. Interact.     Publication Date:  2004 Jan 
Date Detail:
Created Date:  2004-01-16     Completed Date:  2004-03-04     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0227276     Medline TA:  Chem Biol Interact     Country:  Ireland    
Other Details:
Languages:  eng     Pagination:  99-108     Citation Subset:  IM    
Affiliation:
Institute for Inland Water Management and Waste-water Treatment, P.O. Box 17, 8200 AA Lelystad, The Netherlands. a.osman@riza.rws.minvenw.nl
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MeSH Terms
Descriptor/Qualifier:
Animals
Benzoquinones / chemistry,  metabolism*,  pharmacology*
Catalysis / drug effects
Cattle
Hydrophobicity
Kinetics
Liver / enzymology
NAD(P)H Dehydrogenase (Quinone) / isolation & purification,  metabolism*
Rats
Serum Albumin, Bovine / metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Structure-Activity Relationship
Substrate Specificity
Chemical
Reg. No./Substance:
0/Benzoquinones; 0/Serum Albumin, Bovine; EC 1.6.5.2/NAD(P)H Dehydrogenase (Quinone)

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


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