Sulfide-quinone reductase activity in membranes of the chemotrophic bacterium Paracoccus denitrificans GB17

1998 ◽  
Vol 170 (5) ◽  
pp. 353-360 ◽  
Author(s):  
M. Schütz ◽  
Christof Klughammer ◽  
Christoph Griesbeck ◽  
Armin Quentmeier ◽  
Cornelius G. Friedrich ◽  
...  
Keyword(s):  
Paracoccus Denitrificans ◽  
Reductase Activity ◽  
Quinone Reductase

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

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.

The In Vivo Effects of Oral Anticoagulants in Man: Comparison Between Liver and Non-Hepatic Tissues

1988 ◽  
Vol 59 (02) ◽  
pp. 147-150 ◽  
Author(s):  
Marian de Boer-van den Berg ◽  
Henk H W Thijssen ◽  
Cees Vermeer
Keyword(s):  
Vitamin K ◽  
Reductase Activity ◽  
Oral Anticoagulant Therapy ◽  
Oral Anticoagulants ◽  
Quinone Reductase ◽  
Hepatic Microsomes ◽  
Precursor Proteins ◽  
Epoxide Reductase ◽  
In Vivo Effects

SummaryThe in vivo effects of oral anticoagulant therapy with 4–hydroxycoumarins on various vitamin K–dependent enzyme systems in man were compared. In hepatic microsomes obtained from donors who has been treated with 4–hydroxycoumarins for more than 6 months, the vitamin K 2,3 epoxide reductase activity and the DTT–dependent vitamin K quinone reductase activity were diminished to 35% and 20% of the corresponding normal values. In the non–hepatic tissues, only a small decrease in vitamin K 2,3 epoxide reductase activity could be demonstrated, while no differences were found in the vitamin K quinone reductase activities. In none of the tissues a significant increase of non–carboxylated precursor proteins was observed, whereas also vitamin K hydroquinone–dependent carboxylase activities seemed to be unaffected by the anticoagulant treatment.

Effect of hydrogen peroxide on the dehydrogenase and quinone-reductase activity of irradiated Lactobacillus plantarum cells

LWT ◽  
2020 ◽  
Vol 134 ◽  
pp. 110236
Author(s):  
Kristine Kalneniece ◽  
Vasilijs Bankovskis ◽  
Turs Selga ◽  
Toms Kusins ◽  
Inga Balode ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Lactobacillus Plantarum ◽  
Reductase Activity ◽  
Quinone Reductase

scholarly journals The nitric oxide reductase of Paracoccus denitrificans

1990 ◽  
Vol 269 (2) ◽  
pp. 423-429 ◽  
Author(s):  
G J Carr ◽  
S J Ferguson
Keyword(s):  
Nitric Oxide ◽  
Specific Activity ◽  
Paracoccus Denitrificans ◽  
Reductase Activity ◽  
Cytochrome Bc1 Complex ◽  
Horse Heart Cytochrome ◽  
Dodecyl Maltoside ◽  
Solubilized Enzyme ◽  
Horse Heart Cytochrome C ◽  
Good Retention

The nitric oxide (NO) reductase activity of the cytoplasmic membrane of Paracoccus denitrificans can be solubilized in dodecyl maltoside with good retention of activity. The solubilized enzyme lacks NADH-dependent activity, but can be assayed with isoascorbate plus 2,3,5,6-tetramethylphenylene-1,4-diamine as electron donor and with horse heart cytochrome c as mediator. Reduction of NO was measured with an amperomeric electrode. The solubilized enzyme could be separated from other electron-transport components, including the cytochrome bc1 complex and nitrite reductase, by several steps of chromatography. The purified enzyme had a specific activity of 11 mumols.min-1.mg of protein-1 and the Km(NO) was estimated as less than 10 microM. The enzyme formed N2O from NO with the expected stoichiometry. These observations support the view that NO reductase is a discrete enzyme that participates in the denitrification process. The enzyme contained both b- and c-type haems. The former was associated with a polypeptide of apparent molecular mass 37 kDa and the latter with a polypeptide of 18 kDa. Polypeptides of 29 and 45 kDa were also identified in the purified protein which showed variable behaviour on electrophoresis in polyacrylamide gels.

LOT6 from Saccharomyces cerevisiae has an unexpected NAD(P)H-dependent quinone reductase activity

2006 ◽  
Vol 2006 (Spring) ◽  
Author(s):  
Sonja Sollner ◽  
Sigrid Deller ◽  
Heidemarie Ehammer ◽  
Anna Prem ◽  
Peter Macheroux
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Reductase Activity ◽  
Quinone Reductase
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