scholarly journals Remote Amino Acid Recognition Enables Effective Hydrogen Peroxide Activation at a Manganese Oxidation Catalys

2021 ◽  
Author(s):  
Miquel Costas ◽  
Giorgio Olivo ◽  
Laia Vicens
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Manganese Oxidation ◽  
Peroxide Activation ◽  
Effective Hydrogen ◽  
Amino Acid Recognition

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

An ESR study of the peroxidase reaction catalyzed by human methaemoglobin and methaemoglobin-haptoglobin complex

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Peroxidase Activity ◽  
Amino Acid Analysis ◽  
Superoxide Radical ◽  
Esr Spectra ◽  
The Other ◽  
Delocalized Electron

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.

scholarly journals RuIII(edta) mediated oxidation of azide in the presence of hydrogen peroxide. Azide versus peroxide activation

2014 ◽  
Vol 43 (8) ◽  
pp. 3087-3094 ◽  
Author(s):  
Debabrata Chatterjee ◽  
Alicja Franke ◽  
Maria Oszajca ◽  
Rudi van Eldik
Keyword(s):  
Hydrogen Peroxide ◽  
Peroxide Activation ◽  
Mediated Oxidation

Effect of hydrogen peroxide on d-amino acid oxidase from Rhodotorula gracilis

2000 ◽  
Vol 27 (3-5) ◽  
pp. 234-239 ◽  
Author(s):  
Isabel de la Mata ◽  
Fernando Ramón ◽  
Virginia Obregón ◽  
Ma Pilar Castillón ◽  
Carmen Acebal
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Rhodotorula Gracilis

Structural Basis of Furan-Amino Acid Recognition by a Polyspecific Aminoacyl-tRNA-Synthetase and its Genetic Encoding in Human Cells

ChemBioChem ◽  
2014 ◽  
Vol 15 (12) ◽  
pp. 1755-1760 ◽  
Author(s):  
Moritz J. Schmidt ◽  
Annemarie Weber ◽  
Moritz Pott ◽  
Wolfram Welte ◽  
Daniel Summerer
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Human Cells ◽  
Structural Basis ◽  
Aminoacyl Trna Synthetase ◽  
Genetic Encoding ◽  
Amino Acid Recognition

Technical–Economic Analysis of Hydrogen Peroxide Activation by a Sacrificial Anode: Comparison of Two Exchange Membranes

2021 ◽  
Author(s):  
Jhonatan J. Hermosillo-Nevárez ◽  
Yaneth A. Bustos-Terrones ◽  
Jesús G. Rangel-Peraza ◽  
María M. Armendáriz-Ontiveros ◽  
Leonel E. Amábilis-Sosa ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Economic Analysis ◽  
Sacrificial Anode ◽  
Peroxide Activation

Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations 1 1A. R. Fersht

1998 ◽  
Vol 275 (5) ◽  
pp. 823-846 ◽  
Author(s):  
Georgios Archontis ◽  
Thomas Simonson ◽  
Dino Moras ◽  
Martin Karplus
Keyword(s):  
Free Energy ◽  
Amino Acid ◽  
Trna Synthetase ◽  
Specific Amino Acid ◽  
Energy Simulations ◽  
Amino Acid Recognition

scholarly journals Amino acid recognition by fine tuning the association constants: tailored naphthalimides in pillar[5]arene-based indicator displacement assays

RSC Advances ◽  
2016 ◽  
Vol 6 (89) ◽  
pp. 86269-86275 ◽  
Author(s):  
Márton Bojtár ◽  
Adrien Paudics ◽  
Dóra Hessz ◽  
Miklós Kubinyi ◽  
István Bitter
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Association Constants ◽  
Fine Tuning ◽  
Supramolecular Interactions ◽  
Basic Amino Acids ◽  
Anchoring Groups ◽  
Displacement Assays ◽  
Amino Acid Recognition

Three naphthalimide derivatives were synthesized with different anchoring groups to adjust the supramolecular interactions with carboxylato-pillar[5]arene. The complexes were used as indicator displacement assays for basic amino acids and diamines.

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