scholarly journals Histochemical Detection of Quinone Reductase Activity In Situ Using LY 83583 Reduction and Oxidation

2002 ◽  
Vol 70 (5) ◽  
pp. 2156-2164 ◽  
Author(s):  
Timothy H. Murphy ◽  
Austin P. So ◽  
Steve R. Vincent
Keyword(s):  
Reductase Activity ◽  
Quinone Reductase ◽  
Histochemical Detection ◽  
Reduction And Oxidation ◽  
Ly 83583

scholarly journals Svalbamides A and B, Pyrrolidinone-Bearing Lipodipeptides from Arctic Paenibacillus sp.

Marine Drugs ◽  
2021 ◽  
Vol 19 (4) ◽  
pp. 229
Author(s):  
Young Eun Du ◽  
Eun Seo Bae ◽  
Yeonjung Lim ◽  
Jang-Cheon Cho ◽  
Sang-Jip Nam ◽  
...  
Keyword(s):  
Reductase Activity ◽  
Quinone Reductase ◽  
The Arctic ◽  
Amino Acid Residues ◽  
Chemopreventive Agents ◽  
Svalbard Archipelago ◽  
Paenibacillus Sp ◽  
Combinational Analysis ◽  
Culture Extract ◽  
The Absolute

Two new secondary metabolites, svalbamides A (1) and B (2), were isolated from a culture extract of Paenibacillus sp. SVB7 that was isolated from surface sediment from a core (HH17-1085) taken in the Svalbard archipelago in the Arctic Ocean. The combinational analysis of HR-MS and NMR spectroscopic data revealed the structures of 1 and 2 as being lipopeptides bearing 3-amino-2-pyrrolidinone, d-valine, and 3-hydroxy-8-methyldecanoic acid. The absolute configurations of the amino acid residues in svalbamides A and B were determined using the advanced Marfey’s method, in which the hydrolysates of 1 and 2 were derivatized with l- and d- forms of 1-fluoro-2,4-dinitrophenyl-5-alanine amide (FDAA). The absolute configurations of 1 and 2 were completely assigned by deducing the stereochemistry of 3-hydroxy-8-methyldecanoic acid based on DP4 calculations. Svalbamides A and B induced quinone reductase activity in Hepa1c1c7 murine hepatoma cells, indicating that they represent chemotypes with a potential for functioning as chemopreventive agents.

Redox Potentials and Quinone Reductase Activity ofl-Aspartate Oxidase fromEscherichia coli†

Biochemistry ◽  
1997 ◽  
Vol 36 (51) ◽  
pp. 16221-16230 ◽  
Author(s):  
Gabriella Tedeschi ◽  
Lucia Zetta ◽  
Armando Negri ◽  
Michele Mortarino ◽  
Fabrizio Ceciliani ◽  
...  
Keyword(s):  
Reductase Activity ◽  
Quinone Reductase ◽  
Redox Potentials ◽  
Fromescherichia Coli

In situ measurement of HMG-CoA reductase activity in digitonin-permeabilized hepatocytes

1991 ◽  
Vol 180 (2) ◽  
pp. 525-530 ◽  
Author(s):  
Math J.H. Geelen ◽  
Joseph S. Papiez ◽  
Kamal Girgis ◽  
David M. Gibson
Keyword(s):  
Reductase Activity ◽  
In Situ Measurement ◽  
Hmg Coa Reductase ◽  
Coa Reductase

scholarly journals Anaerobic NADH-Fumarate Reductase System Is Predominant in the Respiratory Chain of Echinococcus multilocularis, Providing a Novel Target for the Chemotherapy of Alveolar Echinococcosis

2007 ◽  
Vol 52 (1) ◽  
pp. 164-170 ◽  
Author(s):  
Jun Matsumoto ◽  
Kimitoshi Sakamoto ◽  
Noriko Shinjyo ◽  
Yasutoshi Kido ◽  
Nao Yamamoto ◽  
...  
Keyword(s):  
Respiratory Chain ◽  
Echinococcus Multilocularis ◽  
Alveolar Echinococcosis ◽  
Reductase Activity ◽  
Mitochondrial Respiratory Chain ◽  
Quinone Reductase ◽  
Fumarate Reductase ◽  
Electron Mediator ◽  
Mitochondrial Fractions ◽  
Mitochondrial Respiratory

ABSTRACT Alveolar echinococcosis, which is due to the massive growth of larval Echinococcus multilocularis, is a life-threatening parasitic zoonosis distributed widely across the northern hemisphere. Commercially available chemotherapeutic compounds have parasitostatic but not parasitocidal effects. Parasitic organisms use various energy metabolic pathways that differ greatly from those of their hosts and therefore could be promising targets for chemotherapy. The aim of this study was to characterize the mitochondrial respiratory chain of E. multilocularis, with the eventual goal of developing novel antiechinococcal compounds. Enzymatic analyses using enriched mitochondrial fractions from E. multilocularis protoscoleces revealed that the mitochondria exhibited NADH-fumarate reductase activity as the predominant enzyme activity, suggesting that the mitochondrial respiratory system of the parasite is highly adapted to anaerobic environments. High-performance liquid chromatography-mass spectrometry revealed that the primary quinone of the parasite mitochondria was rhodoquinone-10, which is commonly used as an electron mediator in anaerobic respiration by the NADH-fumarate reductase system of other eukaryotes. This also suggests that the mitochondria of E. multilocularis protoscoleces possess an anaerobic respiratory chain in which complex II of the parasite functions as a rhodoquinol-fumarate reductase. Furthermore, in vitro treatment assays using respiratory chain inhibitors against the NADH-quinone reductase activity of mitochondrial complex I demonstrated that they had a potent ability to kill protoscoleces. These results suggest that the mitochondrial respiratory chain of the parasite is a promising target for chemotherapy of alveolar echinococcosis.

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