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Title Quatenary structure of methemoglobin II. Pulse radiolysis study of the binding of oxygen to the valence-hybrid. Progress report, December 1, 1978-November 30, 1979
Creator/Author Chevion, M. ; Ilan, Y.A. ; Samuni, A. ; Navok, T. ; Czapski, G.
Publication Date1979 Jan 01
OSTI IdentifierOSTI ID: 6137131
Report Number(s)COO-3221-57
DOE Contract NumberEY-76-C-02-3221
Resource TypeTechnical Report
Research OrgHebrew Univ., Jerusalem (Israel)
Subject560111 -- Radiation Effects on Biochemicals-- In Vitro-- (-1987) ;550200 -- Biochemistry ;400600 -- Radiation Chemistry; ;METHEMOGLOBIN-- RADIOLYSIS;METHEMOGLOBIN-- STRUCTURAL CHEMICAL ANALYSIS; AQUEOUS SOLUTIONS;BIOCHEMICAL REACTION KINETICS;CONFIGURATION INTERACTION;EXPERIMENTAL DATA;INOSITOLS;ISOLATED VALUES;OXYGEN;PH VALUE;PHOSPHORIC ACID ESTERS;VALENCE
Related SubjectCARBOHYDRATES;CARBOXYLIC ACIDS;CHEMICAL RADIATION EFFECTS;CHEMICAL REACTIONS;CHEMISTRY;CRYOGENIC FLUIDS;DATA;DATA FORMS;DECOMPOSITION;DISPERSIONS;ELEMENTS;ESTERS;FLUIDS;GLOBIN;HEMOGLOBIN;HETEROCYCLIC ACIDS;HETEROCYCLIC COMPOUNDS;INFORMATION;KINETICS;MIXTURES;MONOSACCHARIDES;NONMETALS;NUMERICAL DATA;ORGANIC ACIDS;ORGANIC COMPOUNDS;ORGANIC NITROGEN COMPOUNDS;ORGANIC PHOSPHORUS COMPOUNDS;PIGMENTS;PORPHYRINS;PROTEINS;RADIATION CHEMISTRY;RADIATION EFFECTS;REACTION KINETICS;SACCHARIDES;SOLUTIONS
Description/Abstract The pulse-radiolysis of solutions of adult human methemoglobin was used in order to reduce a single heme-iron within the protein tetramers.^The valence-hybrids thus formed were reacted with oxygen.^Kinetics of the reactions were studied.^The effects of pH and inositol-hexaphosphate were examined.^The kinetics of the ligation of oxygen to stripped valence-hybrids showed a single-phase behavior at the pH range 6.5 to 9. As the pH was lowered below 6.5 a second, slower phase became apparent.^In the presence of IHP, above pH 8, the kinetics of oxygem binding was of a single phase.^As the pH was lowered a transition to a second, slower phase was noticed.^Below pH 7 the slower phase was the only detectable one.^The analysis of the relative contribution of the faster phase to the total reaction as a function of the pH showed a typical transition curve characterized by a pK = 7.5 and a Hill parameter n =2.9.^On the basis it is concluded that human adult stripped methemoglobin resides in an R quarternary structure while the presence of IHP stabilizes the T structure at pH below 7.5.
Country of PublicationUnited States
LanguageEnglish
FormatPages: 21
AvailabilityDep. NTIS, PC A02/MF A01.
System Entry Date2001 May 13

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