The kinetics of the ClOOCl catalytic cycle

2016 ◽  
Vol 121 (22) ◽  
pp. 13,768-13,783 ◽  
Author(s):  
Timothy P. Canty ◽  
Ross J. Salawitch ◽  
David M. Wilmouth
Keyword(s):  
Catalytic Cycle ◽  
Kinetics Of

Kinetics of the (salen)Cr(iii)- and (salen)Co(iii)-catalyzed copolymerization of epoxides with CO2, and of the accompanying degradation reactions

2015 ◽  
Vol 6 (7) ◽  
pp. 1103-1117 ◽  
Author(s):  
D. J. Darensbourg ◽  
A. D. Yeung
Keyword(s):  
Computational Chemistry ◽  
Product Distribution ◽  
Catalytic Cycle ◽  
Degradation Reactions ◽  
Kinetics Of

The catalytic cycle of the (salen)M(iii)-catalyzed copolymerization for a variety of epoxides with CO2 is elucidated using computational chemistry, and factors that control the kinetics and product distribution of these reactions are described.

scholarly journals Kinetics of the Superoxide Reductase Catalytic Cycle

2003 ◽  
Vol 278 (41) ◽  
pp. 39662-39668 ◽  
Author(s):  
Joseph P. Emerson ◽  
Eric D. Coulter ◽  
Robert S. Phillips ◽  
Donald M. Kurtz
Keyword(s):  
Catalytic Cycle ◽  
Superoxide Reductase ◽  
Kinetics Of

scholarly journals Bioelectrochemical analysis of thermodynamics of the catalytic cycle and kinetics of the oxidative inactivation of oxygen-tolerant [NiFe]-hydrogenase

2016 ◽  
Vol 766 ◽  
pp. 152-161 ◽  
Author(s):  
Keisei So ◽  
Rui Hamamoto ◽  
Ryosuke Takeuchi ◽  
Yuki Kitazumi ◽  
Osamu Shirai ◽  
...  
Keyword(s):  
Catalytic Cycle ◽  
Oxidative Inactivation ◽  
Kinetics Of

scholarly journals The Reaction Kinetics of 3-Hydroxybenzoate 6-Hydroxylase fromRhodococcus jostiiRHA1 Provide an Understanding of thepara-Hydroxylation Enzyme Catalytic Cycle

2013 ◽  
Vol 288 (49) ◽  
pp. 35210-35221 ◽  
Author(s):  
Jeerus Sucharitakul ◽  
Chanakan Tongsook ◽  
Danaya Pakotiprapha ◽  
Willem J. H. van Berkel ◽  
Pimchai Chaiyen
Keyword(s):  
Reaction Kinetics ◽  
Catalytic Cycle ◽  
Kinetics Of

scholarly journals Mathematical Analysis of a Prototypical Autocatalytic Reaction Network

Life ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 42 ◽  
Author(s):  
Ekaterina V. Skorb ◽  
Sergey N. Semenov
Keyword(s):  
Exponential Growth ◽  
Mutual Exclusion ◽  
Reaction Network ◽  
Catalytic Cycle ◽  
Rate Laws ◽  
Experimental Systems ◽  
State Approximation ◽  
Steady State Approximation ◽  
Kinetics Of ◽  
Autocatalytic Networks

Network autocatalysis, which is autocatalysis whereby a catalyst is not directly produced in a catalytic cycle, is likely to be more common in chemistry than direct autocatalysis is. Nevertheless, the kinetics of autocatalytic networks often does not exactly follow simple quadratic or cubic rate laws and largely depends on the structure of the network. In this article, we analyzed one of the simplest and most chemically plausible autocatalytic networks where a catalytic cycle is coupled to an ancillary reaction that produces the catalyst. We analytically analyzed deviations in the kinetics of this network from its exponential growth and numerically studied the competition between two networks for common substrates. Our results showed that when quasi-steady-state approximation is applicable for at least one of the components, the deviation from the exponential growth is small. Numerical simulations showed that competition between networks results in the mutual exclusion of autocatalysts; however, the presence of a substantial noncatalytic conversion of substrates will create broad regions where autocatalysts can coexist. Thus, we should avoid the accumulation of intermediates and the noncatalytic conversion of the substrate when designing experimental systems that need autocatalysis as a source of positive feedback or as a source of evolutionary pressure.

scholarly journals The kinetics of ammonia release during the catalytic cycle of pig plasma amine oxidase

1984 ◽  
Vol 220 (3) ◽  
pp. 767-772 ◽  
Author(s):  
F X Rius ◽  
P F Knowles ◽  
G Pettersson
Keyword(s):  
Time Course ◽  
Amine Oxidase ◽  
Catalytic Cycle ◽  
Sensitive Assay ◽  
Ammonia Release ◽  
Plasma Amine Oxidase ◽  
Kinetics Of ◽  
Enzyme Species

The time course of NH3 release during the catalytic cycle of pig plasma amine oxidase was followed by using the quenched-flow technique in conjunction with a sensitive assay for NH3. These studies were made under both air and O2-saturating conditions. The results establish unequivocally that NH3 is released in the step whereby a reduced enzyme species is re-oxidized by molecular O2 rather than in the step leading to the reduced enzyme. It is concluded that the catalytic cycle of the enzyme conforms to an aminotransferase mechanism rather than one in which an imine is an intermediate.

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