Kinetic and stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide

Toti, Paolo; Petri, Antonella; Gambicorti, Tiziana; Osman, Azizah; Bauer, C.

doi:10.1016/j.bpc.2004.08.003

Cited by 8 publications

(7 citation statements)

References 28 publications

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“…. It is clear that irrespective of the initial G6P and enzyme concentration, a common straight line describes all of the data, which is consistent with Equation (11). Moreover, the intercept on the ordinate ( j b ) is close to zero, confirming the conclusion drawn from Figure 2.…”

Section: Resultssupporting

confidence: 83%

“…Values for the four inactivation rate constants ( j 1 , j 2 , j b and j 4 ) of Equations (11) and (16) have been determined. Although j 3 has not been measured, the fact that j b is zero implies that j 3 ¼ 0, since j b must lie between j 3 and j 4 (Equation 12) and the latter is finite.…”

Section: Discussionmentioning

confidence: 99%

“…Analysis of product formation by G6P dehydrogenase at saturating NAD þ . The data fromFigure 2are plotted according to Equation(11).…”

mentioning

confidence: 99%

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Quantifying the inactivation rate constants for the molecular species comprising the catalytic cycle of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase

Duggleby

2007

Journal of Enzyme Inhibition and Medicinal Chemistry

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When an unstable enzyme is incubated with its substrate(s), catalysis may cease before chemical equilibrium is attained. The residual substrate concentrations depend on their initial concentrations, the initial enzymic activity, and the inactivation rate constants for each molecular species that comprise the catalytic cycle. The underlying theory has been elaborated previously for single-substrate reactions and here it is extended to bi-substrate reactions. The theory is illustrated by application to glucose 6-phosphate dehydrogenase, which is unstable when exposed to a low concentration of sodium dodecyl sulphate. It is shown that the ternary complex containing both substrates is resistant to inactivation while each of the remaining complexes undergoes first-order decay. Rate constants for the inactivation of each complex are calculated.

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Section: Resultssupporting

confidence: 83%

Section: Discussionmentioning

confidence: 99%

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Quantifying the inactivation rate constants for the molecular species comprising the catalytic cycle of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase

Duggleby

2007

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…The time‐course UV–vis spectroscopy is usually employed to study the kinetics of enzyme reactions18 and the phase transition kinetics of conventional thermosensitive copolymers based on N ‐isopropylacrylamide 19, 20…”

Section: Resultsmentioning

confidence: 99%

Thermosensitive phase transition kinetics of poly(N‐isopropylacryl amide‐co‐acrylamide) microgel aqueous dispersions

Wang

Zhao

et al. 2009

J of Applied Polymer Sci

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Thermosensitive poly(N-isopropylacrylamide-co-acrylamide) microgel particles were prepared through precipitation polymerization. The diameters of the microgel particles were in the range of 220-270 nm and showed a monodispersion. The lower critical solution temperatures (LCST) of the microgel dispersions were measured by dynamic light scattering and turbidimetric analysis. The results indicated that the LCST increased with an increase of acrylamide (AAm) content in the copolymer composition. The kinetics of the thermosensitive phase transitions of the microgel particles were investigated by time-course UV-vis spectroscopy. The results indicated that the higher the content of AAm in copolymer composition, the more time is required for equilibrium deswelling and the less time required for equilibrium swelling. In addition, the time required for equilibrium deswelling decreased with an increase of the content of the microgel particles in dispersions. By contrast, the time required for equilibrium swelling increased slightly. Thus, a suitable LCST and time required for equilibrium of phase transition can be achieved by adjusting the molar ratio of the comonomers in the microgels and the content of the microgel particles in dispersions.

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“…The CPO half-life time (t 1/2 ) was experimentally estimated from activity versus time data. Enzymatic activity was determined by the decrease in absorbance at 278 nm due to the conversion of monochlorodimedone (MCD, ε 278 =12.2 mM −1 cm −1 ) 32…”

Section: Cpo Stabilitymentioning

confidence: 99%

Chloroperoxidase-catalyzed amino alcohol oxidation: Substrate specificity and novel strategy for the synthesis of N -Cbz-3-aminopropanal

Masdeu

Pérez‐Trujillo

López-Santı́n

et al. 2016

Process Biochemistry

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This is the author's version of a work that was accepted for publication in Process biochemistry (Elsevier). Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Masdeu, G. et al. "Chloroperoxidase-catalyzed amino alcohol oxidation: substrate specificity and novel strategy for the synthesis of N-Cbz-3-aminopropanal" in

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Kinetic and stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide

Cited by 8 publications

References 28 publications

Quantifying the inactivation rate constants for the molecular species comprising the catalytic cycle of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase

Quantifying the inactivation rate constants for the molecular species comprising the catalytic cycle of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase

Thermosensitive phase transition kinetics of poly(N‐isopropylacryl amide‐co‐acrylamide) microgel aqueous dispersions

Chloroperoxidase-catalyzed amino alcohol oxidation: Substrate specificity and novel strategy for the synthesis of N -Cbz-3-aminopropanal

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