Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5

Biochemistry ◽  
1993 ◽  
Vol 32 (26) ◽  
pp. 6613-6623 ◽  
Author(s):  
Scott H. Northrup ◽  
Kathryn A. Thomasson ◽  
Cynthia M. Miller ◽  
Paul D. Barker ◽  
Lindsay D. Eltis ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ferricytochrome C ◽  
Amino Acid Mutations ◽  
Kinetics Of ◽  
Kinetics Of Reduction

THE REDUCTION OF CYTOCHROMEcBY HYDROQUINONE

1963 ◽  
Vol 41 (1) ◽  
pp. 231-237 ◽  
Author(s):  
G. R. Williams
Keyword(s):  
Reaction Mechanism ◽  
Ionic Strength ◽  
Rate Equation ◽  
Second Order ◽  
Order Rate ◽  
Ferricytochrome C ◽  
Kinetics Of ◽  
Kinetics Of Reduction ◽  
Order Rate Equation

The kinetics of reduction of ferricytochrome c by hydroquinone have been studied. The reaction does not conform to a simple second-order rate equation and it is demonstrated that the deviations are brought about by the presence of p-quinone, one of the products of the reaction. The accelerating effect of p-quinone is explained tentatively on the basis of an involvement of the semi-quinone. The effects on the reaction of pH, ionic strength, and temperature are reported and used to suggest features of the reaction mechanism.

THE REDUCTION OF CYTOCHROMEcBY HYDROQUINONE

1963 ◽  
Vol 41 (1) ◽  
pp. 231-237 ◽  
Author(s):  
G. R. Williams
Keyword(s):  
Reaction Mechanism ◽  
Ionic Strength ◽  
Rate Equation ◽  
Second Order ◽  
Order Rate ◽  
Ferricytochrome C ◽  
Kinetics Of ◽  
Kinetics Of Reduction ◽  
Order Rate Equation

The kinetics of reduction of ferricytochrome c by hydroquinone have been studied. The reaction does not conform to a simple second-order rate equation and it is demonstrated that the deviations are brought about by the presence of p-quinone, one of the products of the reaction. The accelerating effect of p-quinone is explained tentatively on the basis of an involvement of the semi-quinone. The effects on the reaction of pH, ionic strength, and temperature are reported and used to suggest features of the reaction mechanism.

Effects of Some Charged Amino Acid Mutations on the Electron Self-Exchange Kinetics of Cytochromeb5

1999 ◽  
Vol 38 (25) ◽  
pp. 5749-5754 ◽  
Author(s):  
Dejian Ma ◽  
Yibing Wu ◽  
Chengmin Qian ◽  
Wenxia Tang ◽  
Yun-Hua Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Exchange Kinetics ◽  
Amino Acid Mutations ◽  
Kinetics Of

scholarly journals The reduction of carboxymethyl-cytochrome c by chromous ions

1974 ◽  
Vol 141 (2) ◽  
pp. 455-461 ◽  
Author(s):  
Thomas Brittain ◽  
Michael T. Wilson ◽  
Colin Greenwood
Keyword(s):  
Cytochrome C ◽  
Difference Spectrum ◽  
Order Rate Constant ◽  
Stopped Flow ◽  
Methionine Residue ◽  
Ferricytochrome C ◽  
A Charge ◽  
Kinetics Of ◽  
Dependent Processes ◽  
Kinetics Of Reduction

The reduction of ferricytochrome c and ferricytochrome c carboxymethylated at the haem-linked methionine (residue 80) by Cr2+ ions was studied by stopped-flow techniques. At pH6.2 the kinetics of reduction of ferricytochrome c are simple and correspond to a second-order rate constant of 1.21×103m-1·s-1. Under identical conditions the kinetics of reduction of the carboxymethyl derivative, carboxymethyl-cytochrome c, are complex; two Cr2+-concentration-dependent processes (1.5×104m-1·s-1 and 1.3×103m-1·s-1) lead to the formation of an intermediate which decays in monomolecular fashion (0.15s-1) to form the normal fully reduced material. The kinetic difference spectrum for the overall process corresponds to that found statically, whereas the kinetic difference spectrum of the intermediate minus the oxidized form resembles that of the low-spin ferrous form of carboxymethyl-cytochrome c minus oxidized carboxymethyl-cytochrome c. A model is proposed in which the reduction of low-spin ferric carboxymethyl-cytochrome c to high-spin ferrous carboxymethyl-cytochrome c involves a low-spin ferrous intermediate. The monomolecular step involving the decay of this low-spin ferrous intermediate is associated with an activation energy of approx. 126kJ·mol-1 and is thought to involve both a change of spin state and a protein-conformational event. Although carboxymethyl-cytochrome c represents a mixture of species separable on a charge basis, the above observations were independent of which species was chosen for study.

The effect of origin and physico-chemical properties on the kinetics of reduction of mixed NiO-Fe2O3 oxides with hydrogen

1986 ◽  
Vol 51 (10) ◽  
pp. 2098-2108 ◽  
Author(s):  
Milan Pospíšil ◽  
Jan Topinka
Keyword(s):  
Mixed Oxides ◽  
Mutual Influence ◽  
Spinel Phase ◽  
Chemical Properties ◽  
Inhibitory Effect ◽  
Chemical Parameters ◽  
Physico Chemical ◽  
Preliminary Annealing ◽  
Kinetics Of ◽  
Kinetics Of Reduction

We investigated the effect of origin and some physico-chemical parameters on the kinetics of reduction with hydrogen of two series of mixed NiO-Fe2O3 oxides differing by their composition, the character of their precursors (mixed crystalline nitrates and coprecipitated hydroxides) and their decomposition temperature.This effect manifested itself by different magnitudes of specific surfaces of the mixed oxides and coherent regions of present phases as well as by different oxidizing abilities of the surface and differences in morphology and phase composition of corresponding samples in both series investigated. Nonlinear or nonmonotonous composition dependences of physico-chemical parameters investigated point to a mutual influence of individual components, which is also a function of the system origin and which modifies its reactivity during its reduction with hydrogen. The kinetics of the reduction was studied thermogravimetrically at 320-410 °C. The reduction of oxides of the hydroxide origin is catalytically accelerated by primarily reduced nickel, whereas in corresponding samples of the nitrate series, the total NiO is bound to the spinel phase and the reduction is delayed. Experimental IR spectra, the effect of preliminary annealing and DTA of the mixed oxides point to an inhibitory effect of water, which is constitutionally bound in trace admixtures of the goethite phase, on the kinetics of reduction of samples in the hydroxide series.

scholarly journals Genetic Variation and Evolution of the 2019 Novel Coronavirus

2021 ◽  
pp. 1-13
Author(s):  
Salvatore Dimonte ◽  
Muhammed Babakir-Mina ◽  
Taib Hama-Soor ◽  
Salar Ali
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Rapid Evolution ◽  
Single Amino Acid ◽  
Angiotensin Converting Enzyme 2 ◽  
New Type ◽  
Amino Acid Mutations ◽  
Host Infection ◽  
Human Coronaviruses ◽  
Novel Coronavirus

<b><i>Introduction:</i></b> SARS-CoV-2 is a new type of coronavirus causing a pandemic severe acute respiratory syndrome (SARS-2). Coronaviruses are very diverting genetically and mutate so often periodically. The natural selection of viral mutations may cause host infection selectivity and infectivity. <b><i>Methods:</i></b> This study was aimed to indicate the diversity between human and animal coronaviruses through finding the rate of mutation in each of the spike, nucleocapsid, envelope, and membrane proteins. <b><i>Results:</i></b> The mutation rate is abundant in all 4 structural proteins. The most number of statistically significant amino acid mutations were found in spike receptor-binding domain (RBD) which may be because it is responsible for a corresponding receptor binding in a broad range of hosts and host selectivity to infect. Among 17 previously known amino acids which are important for binding of spike to angiotensin-converting enzyme 2 (ACE2) receptor, all of them are conservative among human coronaviruses, but only 3 of them significantly are mutated in animal coronaviruses. A single amino acid aspartate-454, that causes dissociation of the RBD of the spike and ACE2, and F486 which gives the strength of binding with ACE2 remain intact in all coronaviruses. <b><i>Discussion/Conclusion:</i></b> Observations of this study provided evidence of the genetic diversity and rapid evolution of SARS-CoV-2 as well as other human and animal coronaviruses.

Sign in / Sign up

Export Citation Format

Share Document