PMID:12377761: Difference between revisions
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| | !align=left |Citation | ||
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'''Greenleaf, WB and Silverman, DN''' (2002) Activation of the proton transfer pathway in catalysis by iron superoxide dismutase. ''J. Biol. Chem.'' '''277''':49282-6 | |||
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!align=left |Abstract | |||
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Catalysis by Escherichia coli and Porphyromonas gingivalis iron superoxide dismutase was activated by addition of primary amines, as measured by pulse radiolysis and stopped-flow spectrophotometry. This activation was saturable for most amines investigated, and a free energy plot of the apparent second-order rate constant of activation was linear as a function of the pK(a) of the amine, indicating activation by proton transfer. Amines provide an alternate rather than the only pathway for proton transfer, and catalysis was appreciable in the absence of amines. Solvent hydrogen isotope effects were near unity for amine activation, which is consistent with rate-contributing proton transfer if the pK(a) of the proton acceptor on the enzyme is not in the region of the pK(a) values of the amines studied, from 7.8 to 10.6. The activation of catalysis by these amines was uncompetitive with respect to superoxide, interpreted as proton transfer in a ternary complex of amine with the enzyme-bound peroxide dianion. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12377761 PubMed] | |||
Online version:[http://dx.doi.org/10.1074/jbc.M208629200 10.1074/jbc.M208629200] | |||
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|{{ | !align=left |Keywords | ||
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Catalysis; Dose-Response Relationship, Drug; Enzyme Activation; Escherichia coli/enzymology; Ethanol/pharmacology; Hydrogen/chemistry; Hydrogen-Ion Concentration; Isotopes; Models, Chemical; Porphyromonas gingivalis/enzymology; Protein Binding; Protons; Quaternary Ammonium Compounds/pharmacology; Spectrophotometry; Superoxide Dismutase/chemistry; Superoxide Dismutase/metabolism; beta-Alanine/chemistry | |||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:18, 15 September 2013
| Citation |
Greenleaf, WB and Silverman, DN (2002) Activation of the proton transfer pathway in catalysis by iron superoxide dismutase. J. Biol. Chem. 277:49282-6 |
|---|---|
| Abstract |
Catalysis by Escherichia coli and Porphyromonas gingivalis iron superoxide dismutase was activated by addition of primary amines, as measured by pulse radiolysis and stopped-flow spectrophotometry. This activation was saturable for most amines investigated, and a free energy plot of the apparent second-order rate constant of activation was linear as a function of the pK(a) of the amine, indicating activation by proton transfer. Amines provide an alternate rather than the only pathway for proton transfer, and catalysis was appreciable in the absence of amines. Solvent hydrogen isotope effects were near unity for amine activation, which is consistent with rate-contributing proton transfer if the pK(a) of the proton acceptor on the enzyme is not in the region of the pK(a) values of the amines studied, from 7.8 to 10.6. The activation of catalysis by these amines was uncompetitive with respect to superoxide, interpreted as proton transfer in a ternary complex of amine with the enzyme-bound peroxide dianion. |
| Links |
PubMed Online version:10.1074/jbc.M208629200 |
| Keywords |
Catalysis; Dose-Response Relationship, Drug; Enzyme Activation; Escherichia coli/enzymology; Ethanol/pharmacology; Hydrogen/chemistry; Hydrogen-Ion Concentration; Isotopes; Models, Chemical; Porphyromonas gingivalis/enzymology; Protein Binding; Protons; Quaternary Ammonium Compounds/pharmacology; Spectrophotometry; Superoxide Dismutase/chemistry; Superoxide Dismutase/metabolism; beta-Alanine/chemistry |
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