Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Seven fractions sedimenting at between 3000 and 120000g-min were prepared from a rat liver homogenate by differential centrifugation in buffered iso-osmotic sucrose. The following measurements were carried out on each of these fractions: Ruthenium Red-sensitive Ca(2+) transport in the absence and in the presence of P(i) as well as in the presence of N-ethylmaleimide to prevent P(i) cycling, succinate-supported respiration in the absence and in the presence of ADP, the DeltaE and -59 DeltapH components of the protonmotive force, cytochrome oxidase, uncoupler-stimulated adenosine triphosphatase, alpha-glycerophosphate dehydrogenase, P(i) content and the effect on the ;resting' rate of respiration of repeated additions of a fixed Ca(2+) concentration. 2. Ca(2+) transport either in the presence or in the absence of added P(i) and in the presence of N-ethylmaleimide exhibits significantly higher rates in the fraction sedimenting at 8000g-min. By contrast, respiration in the presence or in the absence of added ADP and the values for DeltaE and -59 DeltapH were similar in those fractions sedimenting between 4000 and 20000g-min, indicating that the driving force for Ca(2+) transport was similar in each of these fractions. 3. Experiments designed to determine the capacity of the individual fractions for Ca(2+), as measured by the effect of repeated additions of Ca(2+) on the resting rate of respiration, showed that fraction 2, i.e. that sedimenting at 8000g-min, also exhibited the greatest tolerance towards the uncoupling action of the ion. 4. Of the three enzyme activity profiles, only that of alpha-glycerophosphate dehydrogenase was similar to that of Ca(2+) transport. Because previous workers have assigned this enzyme to loci in the inner peripheral membrane [Werner & Neupert (1972) Eur. J. Biochem.25, 379-396], it is concluded that the Ruthenium Red-sensitive Ca(2+)- transport system also is located in this domain of the inner membrane. The relation of these findings to the mechanisms of mitochondrial Ca(2+) transport and the biogenesis of mitochondria is discussed.
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PMID:Submitochondrial location of ruthenium red-sensitive calcium-ion transport and evidence for its enrichment in a specific population of rat liver mitochondria. 72 72

The potential toxicity of the herbicide Roundup and its fundamental substance (glyphosate) was tested in bioenergetic functions of isolated rat liver mitochondria. Roundup stimulates succinate-supported respiration twice, with simultaneous collapse of transmembrane electrical potential, while glyphosate used in the same concentrations does not induce any significant effect. Additionally, Roundup depresses state 3 respiration by about 40%, at 15 mM, whereas uncoupled respiration in the presence of FCCP is depressed by about 50%. Depression of uncoupled respiratory activity is mediated through partial inhibition of mitochondrial complexes II and III, but not of complex IV. The phosphorylative system was affected by both a direct and an indirect effect on the F0F1 ATPase activity. The addition of uncoupled concentrations of Roundup to Ca2+-loaded mitochondria treated with Ruthenium Red resulted in non-specific membrane permeabilization, as evidenced by mitochondrial swelling in isosmotic sucrose medium. Therefore, the uncoupling of oxidative phosphorylation is also related to the non-specific membrane permeabilization induced by Roundup. Glyphosate alone does not show any relevant effect on the mitochondrial bioenergetics, in opposition to Roundup formulation products. The differences in the toxicity observed could be either attributed to some products of Roundup or to a synergic effect of glyphosate and formulation products. Bearing in mind that mitochondria is provided with a variety of bioenergetic functions mandatory for the regulation of intracellular aerobic energy production and electrolyte homeostasis, these results question the safety of Roundup on animal health.
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PMID:Comparative effects of the Roundup and glyphosate on mitochondrial oxidative phosphorylation. 1626 81

Ruthenium photoreduction methods are described to study electron transfer from cytochrome c to cytochrome c oxidase and within cytochrome oxidase. Methods are described to prepare a ruthenium cytochrome c derivative Ru-39-Cc, by labeling the single sulfhydryl group on horse K39C with (4-bromomethyl-4'methylbipyridine) (bis-bipyridine)ruthenium(II). The ruthenium complex attached to Cys-39 on the opposite side of the heme crevice does not interfere with the interaction with cytochrome oxidase. Laser flash photolysis of a 1:1 complex between Ru-39-Cc and bovine cytochrome oxidase results in photoreduction of heme c within 1 microsec, followed by electron transfer from heme c to Cu(A) in cytochrome oxidase with a rate constant of 60,000 s(-1) and from Cu(A) to heme a with a rate constant of 20,000 s(-1). A new ruthenium dimer, Ru(2)Z, has been developed to reduce Cu(A) within 1 microsec with a yield of 60%, followed by electron transfer from Cu(A) to heme a and then to the heme a(3)/Cu(B) binuclear center. Methods are described to measure the single-electron reduction of each of the intermediates involved in reduction of oxygen to water by cytochrome oxidase, including P(m), F, O(H), and E.
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PMID:Chapter 28 Use of ruthenium photoreduction techniques to study electron transfer in cytochrome oxidase. 1934 7

This review describes the development and application of photoactive ruthenium complexes to study electron transfer and proton pumping reactions in cytochrome c oxidase (CcO). CcO uses four electrons from Cc to reduce O(2) to two waters, and pumps four protons across the membrane. The electron transfer reactions in cytochrome oxidase are very rapid, and cannot be resolved by stopped-flow mixing techniques. Methods have been developed to covalently attach a photoactive tris(bipyridine)ruthenium group [Ru(II)] to Cc to form Ru-39-Cc. Photoexcitation of Ru(II) to the excited state Ru(II*), a strong reductant, leads to rapid electron transfer to the ferric heme group in Cc, followed by electron transfer to Cu(A) in CcO with a rate constant of 60,000s(-1). Ruthenium kinetics and mutagenesis studies have been used to define the domain for the interaction between Cc and CcO. New ruthenium dimers have also been developed to rapidly inject electrons into Cu(A) of CcO with yields as high as 60%, allowing measurement of the kinetics of electron transfer and proton release at each step in the oxygen reduction mechanism.
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PMID:Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidase. 2193 35