Search Results - "Stankovich, M.T"

Determination of glucose oxidase oxidation-reduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms by Stankovich, M T, Schopfer, L M, Massey, V

“…The oxidation-reduction potential values for the two electron transfers to glucose oxidase were obtained at pH 5.3, where the neutral radical is the stable…”
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Oxidation-reduction potentials and ionization states of extracellular peroxidases from the lignin-degrading fungus Phanerochaete chrysosporium by Millis, Cynthia D, Cai, Danying, Stankovich, Marian T, Tien, Ming

“…The oxidation-reduction potentials of lignin peroxidase isozymes H1, H2, H8, and H10 as well as the Mn-dependent peroxidase isozymes H3 and H4 are reported…”
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Roles of component B and reductase in methane monooxygenase (MMO) turnover by Liu, Y., Nesheim, J.C., Paulsen, K.E., Wallar, B.J., Stankovich, M.T., Lipscomb, J.D.

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An electrochemical, kinetic, and spectroscopic characterization of [2Fe-2S] vegetative and heterocyst ferredoxins from Anabaena 7120 with mutations in the cluster binding loop by Weber-Main, A.M, Hurley, J.K, Cheng, H, Xia, B, Chae, Y.K, Markley, J.L, Martinez-Julvez, M, Gomez-Moreno, C, Stankovich, M.T, Tollin, G

“…Residues within the cluster binding loops of plant-type [2Fe-2S] ferredoxins are highly conserved and serve to structurally stabilize this unique region of the…”
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Oxidation-reduction properties of short-chain acyl-CoA dehydrogenase: effects of substrate analogs by Pace, C P, Stankovich, M T

“…Redox potentials of short-chain acyl-CoA dehydrogenase from the anaerobe, Megasphaera elsdenii, have been determined by means of uv-visible…”
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Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver by Husain, M, Stankovich, M.T, Fox, B.G

“…Potentiometric titrations of pig liver electron-transfer flavoprotein (ETF) were performed at pH 7.5 and 4 degrees C, both in the reductive and oxidative…”
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Regulation of oxidation-reduction potentials of anthranilate hydroxylase from Trichosporon cutaneum by substrate and effector binding by Einarsdottir, Gunnlaug H, Stankovich, Marian T, Powlowski, Justin, Ballou, David P, Massey, Vincent

“…The pH dependence of the redox behavior of anthranilate hydroxylase from Trichosporon cutaneum in its uncomplexed and anthranilate-complexed forms, as well as…”
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The effects of reversible freezing inactivation and inhibitor binding on redox properties of L-amino-acid oxidase by Soltysik, S, Byron, C M, Einarsdottir, G H, Stankovich, M T

“…We measured the redox potentials of frozen inactivated L-amino-acid oxidase (L-amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.2) and inhibitor-bound…”
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