scholarly journals Complex I-Associated Hydrogen Peroxide Production Is Decreased and Electron Transport Chain Enzyme Activities Are Altered in n-3 Enriched fat-1 Mice

PLoS ONE ◽  
2010 ◽  
Vol 5 (9) ◽  
pp. e12696 ◽  
Author(s):  
Kevork Hagopian ◽  
Kristina L. Weber ◽  
Darren T. Hwee ◽  
Alison L. Van Eenennaam ◽  
Guillermo López-Lluch ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Electron Transport ◽  
Enzyme Activities ◽  
Complex I ◽  
Electron Transport Chain ◽  
Hydrogen Peroxide Production ◽  
Transport Chain

New inhibitors of Complex I of the mitochondrial electron transport chain with activity as pesticides

1994 ◽  
Vol 22 (1) ◽  
pp. 230-233 ◽  
Author(s):  
Robert M. Hollingworth ◽  
Kabeer I. Ahammadsahib ◽  
G. Gadelhak ◽  
J. L. McLaughlin
Keyword(s):  
Electron Transport ◽  
Complex I ◽  
Electron Transport Chain ◽  
Mitochondrial Electron Transport Chain ◽  
Transport Chain

Formation mechanisms of superoxide radical and hydrogen peroxide in chloroplasts, and factors determining the signalling by hydrogen peroxide

2018 ◽  
Vol 45 (2) ◽  
pp. 102 ◽  
Author(s):  
Boris N. Ivanov ◽  
Maria M. Borisova-Mubarakshina ◽  
Marina A. Kozuleva
Keyword(s):  
Hydrogen Peroxide ◽  
Electron Transport ◽  
Thylakoid Membrane ◽  
Electron Transport Chain ◽  
Superoxide Radical ◽  
Photosynthetic Electron Transport ◽  
Formation Mechanisms ◽  
H2o2 Production ◽  
Photosynthetic Electron Transport Chain ◽  
Transport Chain

Reduction of O2 molecule to superoxide radical, O2•−, in the photosynthetic electron transport chain is the first step of hydrogen peroxide, H2O2, production in chloroplasts in the light. The mechanisms of O2 reduction by ferredoxin, by the components of the plastoquinone pool, and by the electron transfer cofactors in PSI are analysed. The data indicating that O2•− and H2O2 can be produced both outside and within thylakoid membrane are presented. The H2O2 production in the chloroplast stroma is described as a result of either dismutation of O2•− or its reduction by stromal reductants. Formation of H2O2 within thylakoid membrane in the reaction of O2•− with plastohydroquinone is examined. The significance of both ways of H2O2 formation for specificity of the signal being sent by photosynthetic electron transport chain to cell adaptation systems is discussed.

scholarly journals Chemical Genetics Analysis of an Aniline Mustard Anticancer Agent Reveals Complex I of the Electron Transport Chain as a Target

2011 ◽  
Vol 286 (39) ◽  
pp. 33910-33920 ◽  
Author(s):  
Bogdan I. Fedeles ◽  
Angela Y. Zhu ◽  
Kellie S. Young ◽  
Shawn M. Hillier ◽  
Kyle D. Proffitt ◽  
...  
Keyword(s):  
Electron Transport ◽  
Complex I ◽  
Electron Transport Chain ◽  
Anticancer Agent ◽  
Chemical Genetics ◽  
Transport Chain

scholarly journals Oxidation and reduction of pyridine nucleotides in alamethicin-permeabilized plant mitochondria

2004 ◽  
Vol 380 (1) ◽  
pp. 193-202 ◽  
Author(s):  
Fredrik I. JOHANSSON ◽  
Agnieszka M. MICHALECKA ◽  
Ian M. MØLLER ◽  
Allan G. RASMUSSON
Keyword(s):  
Electron Transport ◽  
Complex I ◽  
Electron Transport Chain ◽  
Nadh Dehydrogenase ◽  
Plant Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Intact Cells ◽  
Transport Chain ◽  
Invasive Method

The inner mitochondrial membrane is selectively permeable, which limits the transport of solutes and metabolites across the membrane. This constitutes a problem when intramitochondrial enzymes are studied. The channel-forming antibiotic AlaM (alamethicin) was used as a potentially less invasive method to permeabilize mitochondria and study the highly branched electron-transport chain in potato tuber (Solanum tuberosum) and pea leaf (Pisum sativum) mitochondria. We show that AlaM permeabilized the inner membrane of plant mitochondria to NAD(P)H, allowing the quantification of internal NAD(P)H dehydrogenases as well as matrix enzymes in situ. AlaM was found to inhibit the electron-transport chain at the external Ca2+-dependent rotenone-insensitive NADH dehydrogenase and around complexes III and IV. Nevertheless, under optimal conditions, especially complex I-mediated NADH oxidation in AlaM-treated mitochondria was much higher than what has been previously measured by other techniques. Our results also show a difference in substrate specificities for complex I in mitochondria as compared with inside-out submitochondrial particles. AlaM facilitated the passage of cofactors to and from the mitochondrial matrix and allowed the determination of NAD+ requirements of malate oxidation in situ. In summary, we conclude that AlaM provides the best method for quantifying NADH dehydrogenase activities and that AlaM will prove to be an important method to study enzymes under conditions that resemble their native environment not only in plant mitochondria but also in other membrane-enclosed compartments, such as intact cells, chloroplasts and peroxisomes.

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