Paul Cook to Oxidation-Reduction
This is a "connection" page, showing publications Paul Cook has written about Oxidation-Reduction.
Connection Strength
0.685
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The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH. Arch Biochem Biophys. 2011 Sep 15; 513(2):71-80.
Score: 0.087
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A lysine-tyrosine pair carries out acid-base chemistry in the metal ion-dependent pyridine dinucleotide-linked beta-hydroxyacid oxidative decarboxylases. Biochemistry. 2009 Apr 28; 48(16):3565-77.
Score: 0.074
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Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2008 Apr 01; 47(13):4169-80.
Score: 0.069
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Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum. Biochemistry. 2007 Dec 18; 46(50):14578-88.
Score: 0.067
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Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jun 26; 46(25):7625-36.
Score: 0.065
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Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme. Biochemistry. 1999 Apr 06; 38(14):4398-402.
Score: 0.037
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Oxidative decarboxylation of 6-phosphogluconate by 6-phosphogluconate dehydrogenase proceeds by a stepwise mechanism with NADP and APADP as oxidants. Biochemistry. 1998 Sep 08; 37(36):12596-602.
Score: 0.036
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Secondary tritium and solvent deuterium isotope effects as a probe of the reaction catalyzed by porcine recombinant dihydropyrimidine dehydrogenase. Biochemistry. 1998 Jun 23; 37(25):9156-9.
Score: 0.035
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Metal ion activator effects on intrinsic isotope effects for hydride transfer from decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum. Biochemistry. 1995 Mar 14; 34(10):3253-60.
Score: 0.028
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Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation. Biochemistry. 1994 Mar 01; 33(8):2096-103.
Score: 0.026
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Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction. Biochemistry. 1993 Mar 02; 32(8):1928-34.
Score: 0.024
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Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis. Biochemistry. 1993 Mar 02; 32(8):2036-40.
Score: 0.024
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Acid base catalytic mechanism of the dihydropyrimidine dehydrogenase from pH studies. J Biol Chem. 1993 Feb 15; 268(5):3407-13.
Score: 0.024
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Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction. Biochemistry. 1991 Jun 11; 30(23):5755-63.
Score: 0.021
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Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation. J Biol Chem. 1991 Feb 15; 266(5):2732-8.
Score: 0.021
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pH dependence of kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme. Biochemistry. 1986 Jul 01; 25(13):3752-9.
Score: 0.015
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Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinucleotide-malic enzyme reaction from isotope effects and pH studies. Biochemistry. 1986 Jan 14; 25(1):227-36.
Score: 0.015
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The pH dependence of the reductive carboxylation of pyruvate by malic enzyme. Biochim Biophys Acta. 1985 Jun 10; 829(2):295-8.
Score: 0.014
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Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesis. Anal Biochem. 1979 Jul 15; 96(2):334-40.
Score: 0.002