Results 51 to 60 of about 124,012 (138)

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes [PDF]

open access: yes, 2015
The genomes of three representative Polyporales (Bjerkandera adusta, Phlebia brevispora and a member of the Ganoderma lucidum complex) recently were sequenced to expand our knowledge on the diversity and distribution of genes involved in degradation of ...
Serrano, A.   +3 more
core   +1 more source

Succinate : quinone oxidoreductases from epsilon-proteobacteria [Review] [PDF]

open access: yes, 2002
The epsilon-proteobacteria form a subdivision of the Proteobacteria including the genera Wolinella, Campylobacter, Helicobacter, Sulfurospirillum, Arcobacter and Dehalospirillum.
Lancaster, C. R. D.   +6 more
core   +1 more source

Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centres and membrane attachment [PDF]

open access: yes, 2002
A comprehensive phylogenetic analysis of the core subunits of succinate:quinone oxidoreductases and quinol:fumarate oxidoreductases is performed, showing that the classification of the enzymes as type A to E based on the type of the membrane anchor fully
Pereira, Manuela M   +4 more
core   +1 more source

Exploring malate:quinone oxidoreductases – MQO [PDF]

open access: yes, 2019
"Malate:quinone oxidoreductases (MQOs) are membrane-bound proteins that catalyze the oxidation of malate to oxaloacetate and the reduction of the quinone to quinol.
Pires, Tatiana Clemente
core  

Electrodes modified with lipid membranes to study quinone oxidoreductases

open access: yes, 2009
Quinone oxidoreductases are a class of membrane enzymes that catalyse the oxidation or reduction of membrane-bound quinols/quinones. The conversion of quinone/quinol by these enzymes is difficult to study because of the hydrophobic nature of the enzymes ...
Weiss, SA, Jeuken, LJC
core   +1 more source

Estudo de hidrólise de amidas derivadas do anidrido 2-carbóxi-1,8-naftálico: efeito do grupo vicinal na velocidade e mecanismo de reação / [PDF]

open access: yes, 2000
Tese (doutorado) - Universidade Federal de Santa Catarina, Centro de Ciências Físicas e Matemáticas.A hidrólise dos ácidos 2,8-carbóxi-N,N-dialquilnaftalâmicos, proposta como modelo não mimético de catálise enzimática por proteinases aspárticas, foi ...
Clementin, Rosilene Maria
core  

Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli [PDF]

open access: yes, 2017
Disulfide bond formation is part of the folding pathway for many periplasmic and outer membrane proteins that contain structural disulfide bonds. In Escherichia coli, a broad variety of periplasmic protein thiol:disulfide oxidoreductases have been ...
Hennecke, Hauke   +2 more
core  

Deep evolutionary conservation of an intramolecular protein kinase activation mechanism [PDF]

open access: yes, 2012
DYRK-family kinases employ an intramolecular mechanism to autophosphorylate a critical tyrosine residue in the activation loop. Once phosphorylated, DYRKs lose tyrosine kinase activity and function as serine/threonine kinases.
Cleghon Vaughn   +31 more
core   +1 more source

Efeito de grupos espectadores na hidrólise de diésteres fosfóricos. Estudos da hidrílise do bis-2-piridil fosfato e das reações do fármaco deferoxamina com mono-e triéster de fosfato [PDF]

open access: yes, 2013
Tese (doutorado) - Universidade Federal de Santa Catarina, Centro de Ciências Físicas e Matemáticas, Programa de Pós-Graduação em Química, Florianópolis, 2013.Esta tese de doutoramento compreende: (i) Estudo das reações de deferoxamina (DFO) com 2,4 ...
Medeiros, Michelle
core  

Protein disulphide oxidoreductases in bacteria.

open access: yes, 1994
Thioredoxins and eukaryotic protein disulphide isomerases were, until recently, the only enzymes known to catalyse reversible oxidation and reduction of cysteine residues of a wide spectrum of protein substrates. Genetic and biochemical investigations on
Hennecke H, Loferer H
core   +1 more source

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