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Journal ArticleDOI

Sites of inhibition of mitochondrial electron transport by cadmium.

Stefania Miccadei, +1 more
- 01 Dec 1993 - 
- Vol. 89, pp 159-167
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TLDR
Spectroscopic evidence demonstrates that cadmium induces an oxidation of NAD(P)H in mitochondria in states 1 and 4 and prevents the reduction of mitochondrial NAD( P)+ by substrates, thus indicating that the site must be localized between NAD-linked substrates and respiratory chain.
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This article is published in Chemico-Biological Interactions.The article was published on 1993-12-01. It has received 107 citations till now. The article focuses on the topics: Cytochrome C1 & Cytochrome c oxidase.

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Citations
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Journal ArticleDOI

Cadmium inhibits the electron transfer chain and induces reactive oxygen species.

TL;DR: The results of kinetic studies and electron turnover experiments suggest that Cd may bind between semiubiquinone and cy tochrome b566 of the Q0 site of cytochrome b of complex III, resulting in accumulation of semiUBiquinones at theQ0 site, providing a possible mechanism for Cd-induced generation of ROS in mitochondria.
Journal ArticleDOI

Origin of cadmium-induced reactive oxygen species production: mitochondrial electron transfer versus plasma membrane NADPH oxidase.

TL;DR: The immediate consequence of exposure to Cd(2+) in vivo is stimulation of ROS production in the mitochondrial electron transfer chain and inhibition of NADPH oxidase activity in the plasma membrane.
Journal ArticleDOI

The plant MT1 metallothioneins are stabilized by binding cadmiums and are required for cadmium tolerance and accumulation.

TL;DR: The ancient class of MT1 protein sequences may be preserved in plant genomes, because it has distinct metal-binding properties, confers tolerance to cadmium, and can assist with zinc homeostasis.
Journal ArticleDOI

Cadmium and mitochondria.

TL;DR: This review provides new additional informations on the cellular and molecular aspects of the interaction between Cd and cells, emphasizing alterations of mitochondria as important events in Cd cytotoxicity, thus representing an important basis for understanding the mechanisms of cadmium effect on the cells.
Journal ArticleDOI

Cadmium effects on mitochondrial function are enhanced by elevated temperatures in a marine poikilotherm, Crassostrea virginica Gmelin (Bivalvia: Ostreidae).

TL;DR: In this article, the combined effects of cadmium and elevated temperature on mitochondrial function in oysters were studied in response to different Cadmium levels and temperatures in isolated mitochondria from the eastern oyster Crassostrea virginica acclimated at 15°C.
References
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Journal ArticleDOI

Determination of serum proteins by means of the biuret reaction.

TL;DR: An investigation of the biochemical changes following experimental liver injury felt the need of a simple, rapid, and accurate method for determining the protein fractions in small amounts of serum and began with Kingsley’s biuret procedure.
Journal ArticleDOI

Uncoupling of oxidative phosphorylation by cadmium ion

TL;DR: Rabbit liver mitochondria used only for the experiments in Table I were prepared by grinding the tissue in 0.25 M sucrose in a Waring blendor at reduced speed and suspended in 1 ml.
Book ChapterDOI

Preparation and characterization of mitochondria and submitochondrial particles of rat liver and liver-derived tissues.

TL;DR: The chapter represents the most detailed account of preparative procedures available for mitochondria and submitochondrial particles of rat liver and presents flow diagrams that include many of the methods to obtain an overall view of a given procedure.
Journal ArticleDOI

O2 solubility in aqueous media determined by a kinetic method

TL;DR: In the method described the rates of O2 and H+ uptake are precisely linear and stoichiometric when NADH is present in large excess over O2, but when O2 is in excess and small additions of 340-nm-standardized NADH are made, as in earlier methods based on NADH oxidation, the endpoint is approached very gradually and tends to overestimate O2 solubility.
Journal ArticleDOI

Action of the antitumor and antispermatogenic agent lonidamine on electron transport in ehrlich ascites tumor mitochondria.

TL;DR: Spectroscopic experiments suggest that electron transport in tumor mitochondria is inhibited by lonidamine at the dehydrogenase-coenzyme level, particularly when the electron carriers are in a relatively oxidized state and/or when the inner membrane-matrix compartment is in the condensed state.
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