Reactivation of the NADH-Q1 reductase activity of the isolated rotenone-insensitive NADH dehydrogenase of Arum maculatum mitochondria. Activation of quinone reductase activity by a hydrophobic component extractable from Arum mitochondrial membranes

Plant Science ◽  
1985 ◽  
Vol 42 (2) ◽  
pp. 73-76 ◽  
Author(s):  
Neil D. Cook ◽  
Richard Cammack
Keyword(s):  
Nadh Dehydrogenase ◽  
Reductase Activity ◽  
Quinone Reductase ◽  
Mitochondrial Membranes ◽  
Hydrophobic Component ◽  
Arum Maculatum

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.

scholarly journals FINE STRUCTURE OF LIPID-DEPLETED MITOCHONDRIA

1967 ◽  
Vol 32 (1) ◽  
pp. 193-208 ◽  
Author(s):  
Sidney Fleischer ◽  
Becca Fleischer ◽  
Walther Stoeckenius
Keyword(s):  
Fine Structure ◽  
Reductase Activity ◽  
Aqueous Acetone ◽  
Unit Membrane ◽  
Mitochondrial Membranes ◽  
Inner Membrane ◽  
Thin Sections ◽  
Membrane Particles ◽  
Succinate Cytochrome C Reductase ◽  
Many Particles

The fine structure of mitochondria and submitochondrial vesicles depleted of their lipid by extraction with aqueous acetone was studied. Thin sections of mitochondrial membranes depleted of more than 95% of their lipid retained the unit membrane structure. Densitometer tracings of the electron micrographs showed that the unit membrane of extracted mitochondria was, on the average, wider than that of unextracted controls and showed a greater variation in width. The outer membrane was lost in mitochondria from which 80–95% of the lipids was extracted. Inner membrane particles were present on submitochondrial vesicles depleted of up to 85% of their lipids. However, when more than 95% of the lipid was removed, few, if any, particles remained attached to the membranes but many particles were found unattached in the background. When lipid was restored to lipid-deficient preparations, the mitochondrial membranes were found to be devoid of inner membrane particles but were fully active with respect to succinate-cytochrome c reductase activity.

A new water-soluble bacterial NADH: fumarate oxidoreductase

2020 ◽  
Vol 367 (20) ◽  
Author(s):  
Yulia V Bertsova ◽  
Ilya P Oleynikov ◽  
Alexander V Bogachev
Keyword(s):  
Nadh Dehydrogenase ◽  
Reductase Activity ◽  
Domain Architecture ◽  
Water Soluble ◽  
Fumarate Reductase ◽  
Anaerobic Conditions ◽  
New Type ◽  
Prosthetic Groups ◽  
Low Rate ◽  
Covalently Bound

ABSTRACT The cytoplasmic fumarate reductase of Klebsiella pneumoniae (FRD) is a monomeric protein which contains three prosthetic groups: noncovalently bound FMN and FAD plus a covalently bound FMN. In the present work, NADH is revealed to be an inherent electron donor for this enzyme. We found that the fumarate reductase activity of FRD significantly exceeds its NADH dehydrogenase activity. During the catalysis of NADH:fumarate oxidoreductase reaction, FRD turnover is limited by a very low rate (∼10/s) of electron transfer between the noncovalently and covalently bound FMN moieties. Induction of FRD synthesis in K. pneumoniae cells was observed only under anaerobic conditions in the presence of fumarate or malate. Enzymes with the FRD-like domain architecture are widely distributed among various bacteria and apparently comprise a new type of water-soluble NADH:fumarate oxidoreductases.

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
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