Mechanistic studies on the reversible binding of nitric oxide to metmyoglobin

2001
journal article
article
150
cris.lastimport.wos2024-04-10T01:52:02Z
dc.abstract.enThe ferriheme protein metmyoglobin (metMb) in buffer solution at physiological pH 7.4 reversibly binds the biomessenger molecule nitric oxide to yield the nitrosyl adduct (metMb(NO)). The kinetics of the association and dissociation processes were investigated by both laser flash photolysis and stopped-flow kinetics techniques at ambient and high pressure, in three laboratories using several different sources of metMb. The activation parameters $\Delta$H⧧, $\Delta$S⧧, and $\Delta$V⧧ were calculated from the kinetic effects of varying temperature and hydrostatic pressure. For the "on" reaction of metMb plus NO, reasonable agreement was found between the various techniques with $\Delta$$H_{on}$⧧, $\Delta$$S_{on}$⧧, and $\Delta$$V_{on}$⧧ determined to have the respective values $\sim65$ kJ $mol^{-1}$, $\sim60$ J $mol^{-1}$ $K^{-1}$, and $\sim20$ $cm^{3}$ $mol^{-1}$. The large and positive $\Delta$S⧧ and $\Delta$V⧧ values are consistent with the operation of a limiting dissociative ligand substitution mechanism whereby dissociation of the $H_{2}O$ occupying the sixth distal coordination site of metMb must precede formation of the Fe-NO bond. While the activation enthalpies of the "off" reaction displayed reasonable agreement between the various techniques (ranging from 68 to 83 kJ $mol^{-1}$), poorer agreement was found for the $\Delta$$S_{off}$⧧ values. For this reason, the kinetics for the "off" reaction were determined more directly via NO trapping experiments, which gave the respective activation parameters $\Delta$$H_{off}$⧧ = 76 kJ $mol^{-1}$, $\Delta$$S_{off}$⧧ = $\sim41$ J $mol^{-1}$ $K^{-1}$, and $\Delta$$V_{off}$⧧ = 20 $cm^{3}$ $mol^{-1}$), again consistent with a limiting dissociative mechanism. These results are discussed in reference to other investigations of the reactions of NO with both model systems and metalloproteins.pl
dc.affiliationWydział Chemii : Zakład Chemii Nieorganicznejpl
dc.contributor.authorLaverman, Leroy E.pl
dc.contributor.authorWanat, Alicjapl
dc.contributor.authorOszajca, Januszpl
dc.contributor.authorStochel, Grażyna - 132108 pl
dc.contributor.authorFord, Peter C.pl
dc.contributor.authorvan Eldik, Rudi - 239234 pl
dc.date.accessioned2015-08-26T10:15:18Z
dc.date.available2015-08-26T10:15:18Z
dc.date.issued2001pl
dc.description.admin[AU] van Eldik, Rudi [SAP14007947]pl
dc.description.number2pl
dc.description.physical285-293pl
dc.description.volume123pl
dc.identifier.doi10.1021/ja001696zpl
dc.identifier.eissn1520-5126pl
dc.identifier.issn0002-7863pl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/15048
dc.languageengpl
dc.language.containerengpl
dc.rightsDodaję tylko opis bibliograficzny*
dc.rights.licenceBez licencji otwartego dostępu
dc.rights.uri*
dc.subtypeArticlepl
dc.titleMechanistic studies on the reversible binding of nitric oxide to metmyoglobinpl
dc.title.journalJournal of the American Chemical Societypl
dc.typeJournalArticlepl
dspace.entity.typePublication
cris.lastimport.wos
2024-04-10T01:52:02Z
dc.abstract.enpl
The ferriheme protein metmyoglobin (metMb) in buffer solution at physiological pH 7.4 reversibly binds the biomessenger molecule nitric oxide to yield the nitrosyl adduct (metMb(NO)). The kinetics of the association and dissociation processes were investigated by both laser flash photolysis and stopped-flow kinetics techniques at ambient and high pressure, in three laboratories using several different sources of metMb. The activation parameters $\Delta$H⧧, $\Delta$S⧧, and $\Delta$V⧧ were calculated from the kinetic effects of varying temperature and hydrostatic pressure. For the "on" reaction of metMb plus NO, reasonable agreement was found between the various techniques with $\Delta$$H_{on}$⧧, $\Delta$$S_{on}$⧧, and $\Delta$$V_{on}$⧧ determined to have the respective values $\sim65$ kJ $mol^{-1}$, $\sim60$ J $mol^{-1}$ $K^{-1}$, and $\sim20$ $cm^{3}$ $mol^{-1}$. The large and positive $\Delta$S⧧ and $\Delta$V⧧ values are consistent with the operation of a limiting dissociative ligand substitution mechanism whereby dissociation of the $H_{2}O$ occupying the sixth distal coordination site of metMb must precede formation of the Fe-NO bond. While the activation enthalpies of the "off" reaction displayed reasonable agreement between the various techniques (ranging from 68 to 83 kJ $mol^{-1}$), poorer agreement was found for the $\Delta$$S_{off}$⧧ values. For this reason, the kinetics for the "off" reaction were determined more directly via NO trapping experiments, which gave the respective activation parameters $\Delta$$H_{off}$⧧ = 76 kJ $mol^{-1}$, $\Delta$$S_{off}$⧧ = $\sim41$ J $mol^{-1}$ $K^{-1}$, and $\Delta$$V_{off}$⧧ = 20 $cm^{3}$ $mol^{-1}$), again consistent with a limiting dissociative mechanism. These results are discussed in reference to other investigations of the reactions of NO with both model systems and metalloproteins.
dc.affiliationpl
Wydział Chemii : Zakład Chemii Nieorganicznej
dc.contributor.authorpl
Laverman, Leroy E.
dc.contributor.authorpl
Wanat, Alicja
dc.contributor.authorpl
Oszajca, Janusz
dc.contributor.authorpl
Stochel, Grażyna - 132108
dc.contributor.authorpl
Ford, Peter C.
dc.contributor.authorpl
van Eldik, Rudi - 239234
dc.date.accessioned
2015-08-26T10:15:18Z
dc.date.available
2015-08-26T10:15:18Z
dc.date.issuedpl
2001
dc.description.adminpl
[AU] van Eldik, Rudi [SAP14007947]
dc.description.numberpl
2
dc.description.physicalpl
285-293
dc.description.volumepl
123
dc.identifier.doipl
10.1021/ja001696z
dc.identifier.eissnpl
1520-5126
dc.identifier.issnpl
0002-7863
dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/15048
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Dodaję tylko opis bibliograficzny
dc.rights.licence
Bez licencji otwartego dostępu
dc.rights.uri*
dc.subtypepl
Article
dc.titlepl
Mechanistic studies on the reversible binding of nitric oxide to metmyoglobin
dc.title.journalpl
Journal of the American Chemical Society
dc.typepl
JournalArticle
dspace.entity.type
Publication
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