Document Detail


Interaction of reactive oxygen and nitrogen species with albumin- and methemoglobin-bound dinitrosyl-iron complexes.
MedLine Citation:
PMID:  18036856     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Destructive effect of superoxide anions O2- derived from KO(2) or xanthine-xanthine oxidase system on dinitrosyl-iron complexes bound with bovine albumin or methemoglobin (DNIC-BSA or DNIC-MetHb) was demonstrated. The sensitivity of DNIC-BSA synthesized by the addition of DNIC with cysteine, thiosulfate or phosphate (DNIC-BSA-1, DNIC-BSA-2 or DNIC-BSA-3, respectively) to destructive action of O2- decreased in row: DNIC-BSA-1>DNIC-BSA-3>DNIC-BSA-2. The estimated rate constant for the reaction between O2- and DNIC-BSA-3 was equal to approximately 10(7)M(-1)s(-1). However, hydrogen peroxide and tert-butyl hydrogenperoxide (t-BOOH) did not induce any noticeable degradation of DNIC-BSA-3 even when used at concentrations exceeding by one order of magnitude those of the complex. As to their action on DNIC-MetHb both hydrogen peroxide and t-BOOH-induced rapid degradation of the complex. Both agents could induce the process due to the effect of alkylperoxyl or protein-derived free radicals formed at the interaction of the agents with ferri-heme groups of MetHb. Peroxynitrite (ONOO(-)) could also initiate protein-bound DNIC degradation more efficiently in the reaction with DNIC-BSA-3. Higher resistance of DNIC-MetHb to peroxynitrite was most probably due to the protective action of heme groups on ONOO(-). However, the analysis allows to suggest that the interaction of protein-bound DNICs with O2- is the only factor responsible for the degradation of the complexes in cells and tissues.
Authors:
Konstantin B Shumaev; Andrey A Gubkin; Vladimir A Serezhenkov; Irina I Lobysheva; Olga V Kosmachevskaya; Enno K Ruuge; Vadim Z Lankin; Alexey F Topunov; Anatoly F Vanin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-10-01
Journal Detail:
Title:  Nitric oxide : biology and chemistry / official journal of the Nitric Oxide Society     Volume:  18     ISSN:  1089-8603     ISO Abbreviation:  Nitric Oxide     Publication Date:  2008 Feb 
Date Detail:
Created Date:  2007-12-31     Completed Date:  2008-05-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9709307     Medline TA:  Nitric Oxide     Country:  United States    
Other Details:
Languages:  eng     Pagination:  37-46     Citation Subset:  IM    
Affiliation:
Russian Cardiological Research-and-Production Complex, Moscow, Russian Federation.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cattle
Hydrogen Peroxide / chemistry
Iron / chemistry*
Methemoglobin / chemistry*
Nitrogen Oxides / chemistry*
Peroxynitrous Acid / chemistry
Reactive Nitrogen Species / chemistry*
Reactive Oxygen Species / chemistry*
Serum Albumin, Bovine / chemistry*
Time Factors
tert-Butylhydroperoxide / chemistry
Chemical
Reg. No./Substance:
0/Nitrogen Oxides; 0/Reactive Nitrogen Species; 0/Reactive Oxygen Species; 0/Serum Albumin, Bovine; 14691-52-2/Peroxynitrous Acid; 68586-27-6/dinitrosyl iron complex; 7439-89-6/Iron; 75-91-2/tert-Butylhydroperoxide; 7722-84-1/Hydrogen Peroxide; 9008-37-1/Methemoglobin

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


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