Kinetic studies on the reaction of NO with iron(ii) complexes using low temperature stopped-flow techniques

2020 ◽  
Vol 49 (27) ◽  
pp. 9480-9486
Author(s):  
Pascal Specht ◽  
Martin Oßberger ◽  
Peter Klüfers ◽  
Siegfried Schindler
Keyword(s):  
Low Temperature ◽  
Kinetic Study ◽  
Reaction Mechanisms ◽  
Kinetic Studies ◽  
Stopped Flow ◽  
Flow Techniques

Quite different reaction mechanisms were observed in a kinetic study of NO binding to iron(ii) complexes.

Reaktionskinetische Untersuchungen zur Bildung von Carbeniumionen des Triphenylmethyl-Typs / Kinetic Investigations of the Formation of Carbenium Ions of the Triphenylmethyl Type

1975 ◽  
Vol 30 (7-8) ◽  
pp. 561-565 ◽  
Author(s):  
Matthias Walper ◽  
Hans-Dieter Brauer ◽  
Hartwig Kelm
Keyword(s):  
Acetic Acid ◽  
Acid Concentration ◽  
Rate Constants ◽  
Reaction Mechanisms ◽  
Stopped Flow ◽  
Carbenium Ions ◽  
Kinetic Investigations ◽  
Flow Techniques

The rates of formation of three mono- and three dicarbenium ions of the triphenylmethyl type from the corresponding carbinols in trifluoro acetic acid - toluene mixtures were investigated using stopped flow techniques.The reaction mechanisms are discussed in view of the obtained dependencies of the rate constants on acid concentration and temperature.

scholarly journals Kinetic studies on (N-formyltryptophyl)cytochrome c

1975 ◽  
Vol 149 (3) ◽  
pp. 713-717 ◽  
Author(s):  
T Brittain ◽  
C Greenwood
Keyword(s):  
Cytochrome C ◽  
Flash Photolysis ◽  
Reduction Process ◽  
Kinetic Studies ◽  
Tryptophan Residue ◽  
Kinetic Properties ◽  
Stopped Flow ◽  
Normal Environment ◽  
Two Phases ◽  
Flow Techniques

The formylation of the ring nitrogen atom of the tryptophan residue in cytochrome c was carried out and consequent changes in the kinetic properties of the protein were investigated. The reduction of formylated cytochrome c by Cr2+ was studied by stopped-flow techniques. At pH 6.5 the reduction process shows the presence of two phases. One phase (k = 4 × 104 M-1-s-1) is dependent on Cr2+ concentration and one phase (k = 5.0 s-1) is not. A study of the temperature dependence of the two phases yields values for their activation energies of 38.6kJ·mol-1 and 42.4kJ·mol-1 respectively. The reaction of the reduced formylated cytochrome c with CO was followed by means of both stopped-flow techniques and flash photolysis. The combination with CO at pH 6.8 measured in stopped-flow experiments shows two phases, both dependent on the concentration of CO (k1 = 1.8 × 102 M-1-s-1). If CO was dissociated from the protein by photolysis and then allowed to recombine with it, it was found to do so in a simple manner, at a rate which depended on the concentration of CO (k = 1.9 × 10M2 M-1-s-1). A tentative model which can accommodate these findings is proposed. The reaction of the oxidized form of formylated cytochrome c with NO was followed by means of stopped-flow techniques. The reaction was found to be biphasic with one phase dependent on the concentration of NO (k = 2.8 × 103 M-1-s-1) and one phase (k = 0.2s-1) independent of the concentration of NO. This behaviour is compared with that of the native molecule. A comparison of these kinetic observations with those on other tryptophan-specific modifications leads to the conclusion that the main alteration in kinetic properties is due, not to the nature of the modifying group, but rather to the disruption of the normal environment of the haem.

Reaction mechanisms involving the hydroxyl radical in the low-temperature oxidation of coal

Fuel ◽  
2021 ◽  
pp. 122732
Author(s):  
Zhilin Xi ◽  
Mengmeng Li ◽  
Xue Li ◽  
Linping Lu ◽  
Jiawei Wang
Keyword(s):  
Low Temperature ◽  
Hydroxyl Radical ◽  
Reaction Mechanisms ◽  
Low Temperature Oxidation ◽  
Temperature Oxidation

scholarly journals Stopped-flow kinetic study of the H2O2 oxidation of substrates catalyzed by microperoxidase-8

2001 ◽  
Vol 6 (8) ◽  
pp. 770-777 ◽  
Author(s):  
Hui-Chun Yeh ◽  
Jinn-Shyan Wang ◽  
Oliver Y. Su ◽  
Wann-Yin Lin
Keyword(s):  
Kinetic Study ◽  
Stopped Flow ◽  
H2o2 Oxidation ◽  
Microperoxidase 8
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