The effect of plague murine toxin on the electron-transport system

Kadis, Solomon; Cohen, Murray; Ajl, Samuel J.

doi:10.1016/0005-2787(65)90581-2

Cited by 8 publications

(6 citation statements)

References 10 publications

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“…Investigation of the murine toxin of Pasteurella pestis revealed that the impairment of mitochondrial respiration was due to the action of the toxin on the electron-transport chain between NADH2 or succinate and cytochrome b, and more specifically at the level of NADH2-ubiquinone reductase (Ajl, Woebke and Rust, 1958;Kadis, Cohen and Ajl, 1965;Kadis, Montie and Ajl, 1966). Neufeld, Coleman and Zannucci (1963) isolated an inhibitor from Serratia marcescens that had an action similar to that of the 2-alkyl-4-hydroxyquinoline-N-oxides isolated from Ps.…”

Section: Ubiquinonementioning

confidence: 99%

The Site Of The Activity Of Extracellular Products Of Pseudomonas Aeruginosa In The Electron-Transport Chain In Mammalian Cell Respiration

Stewart‐Tull

1971

Journal of Medical Microbiology

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IN a previous communication Armstrong, Stewart-Tull and Roberts (1971) found that 1-hydroxyphenazine inhibited the uptake of oxygen by mouse-liver mitochondria.The 1 -hydroxyphenazine was either chemically synthesised or prepared from a biological sample of pyocyanin obtained previously from the culture filtrate of Pseudomonas aeruginosa NCTC6750. The inhibition was not significant with pyrogallol monomethylether, l-methoxyphenazine or pyocyanin. Although numerous lines of research were followed for many years the exact mode of action of pyocyanin and its phenazine derivatives on cellular respiration has not been determined. Pyocyanin has been described as an electron donor and acceptor, a terminal oxidase and an inhibitor, all of these functions taking place at different sites along the chain (Keilin and Hartree, 1940;Anderson, 1946;Hewitt, 1950;Mahler and Cordes, 1968). Lightbown and Jackson (1 956) isolated 2-alkyl-4-hydroxyquinoline-Noxides from Ps. aeruginosa and showed that they were potent inhibitors of succinic oxidase acting between cytochrome b and c in the electron-transport chain.The purpose of the present investigation was to determine the site of activity in the electron-transport chain of 1-hydroxyphenazine, derived from Ps. aeruginosa or chemically synthesised. MATERIALS AND METHODSPseudomonas fractions and mouse-liver mitochondria1 suspensions. These were prepared according to the methods outlined by Armstrong et al.The efect of pseudomonas fractions at the site of succinic dehydrogenase. Thunberg tubes were set up containing 1.4 ml Hendry's sucrose phosphate buffer (I), 0.5 ml mouseliver mitochondria1 suspension, 0.5 ml pseudomonas fraction in the tube and 0-3 ml 0 -2~ sodium succinate plus 0.3 ml 0.001~ methylene blue in the side-arm; controls were set up without a pseudomonas fraction. After equilibration to 37°C the contents of the side-arm were tipped into the evacuated tube and the time required for 90 per cent. reduction of the dye was taken as a measure of dehydrogenase activity.The eflect ofpseudomonas fractions at the site of cytochrome oxidase. This was measured manometrically in the Warburg apparatus by the standard method described by Armstrong et al., with the exception that paraphenylenediamine (16.24 mg per ml buffer I) or 0 . 2~ sodium succinate was the substrate. To further investigate any activity at this site 0.3 ml cytochrome c (2.4 mg per ml buffer I; Koch-Light Laboratories Ltd) was added from the second side-arm to mitochondria respiring on sodium succinate and treated with a pseudomonas fraction.

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Section: Ubiquinonementioning

confidence: 99%

The Site Of The Activity Of Extracellular Products Of Pseudomonas Aeruginosa In The Electron-Transport Chain In Mammalian Cell Respiration

Stewart‐Tull

1971

Journal of Medical Microbiology

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“…Since the toxin inhibited mitochondrial respiration but did not interfere with oxidative phosphorylation, it appeared logical that the toxin might exert its effect on the electron transport system. Kadis et al (36) reported that, although the toxin inhibited the oxidation of a-ketoglutarate, succinate, malate, and fl-hydroxybutyrate in the presence of ADP as phosphate acceptor, the percentage inhibition was, in no case, altered upon the addition of 2,4-dinitrophenol. In this respect the toxin did not behave, for example, like oligomycin, a classical inhibitor of oxidative phosphorylation.…”

Section: Action Of the Toxin On Mammalian Mitochondriamentioning

confidence: 99%

“…Confirmatory evidence on this point was obtained. The toxin had no effect on the oxidation of ascorbate by rat heart or liver mitochondria in the presence of tetramethylphenylenediamine I on September 30, 2020 by guest http://mmbr.asm.org/ Downloaded from (TMPD) or cytochrome c as electron carriers (36). Since TMPD serves as a mobile electron carrier between ascorbate and members of the respiratory chain and acts between cytochrome c and oxygen (20), it appears that the toxin has no effect on the area of the electron transport system between cytochrome c and oxygen.…”

Section: Action Of the Toxin On Mammalian Mitochondriamentioning

confidence: 99%

“…That this was not the case was suggested by the finding that the toxin inhibits the ATP-supported accumulation of Ca++ and Pi by rat heart mitochondria in the absence of a respiratory substrate. Additional evidence on this point stemmed from the fact that, although toxin had no effect on the respiration of rat heart mitochondria in the presence of ascorbate and TMPD (36,37), it inhibited the uptake of Ca++ and Pi supported by this segment of the electron transfer chain.…”

Section: Action Of the Toxin On Mammalian Mitochondriamentioning

confidence: 99%

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The murine toxin of Pasteurella pestis: a study in its development.

Kadis¹,

Montie²,

Ajl³

1966

Bacteriological Reviews

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“…Confirmatory evidence on this point was obtained. The toxin had no effect on the oxidation of ascorbate by rat heart or liver mitochondria in the presence of tetramethylphenylenediamine I on December 13, 2020 by guest http://mmbr.asm.org/ Downloaded from (TMPD) or cytochrome c as electron carriers (36). Since TMPD serves as a mobile electron carrier between ascorbate and members of the respiratory chain and acts between cytochrome c and oxygen (20), it appears that the toxin has no effect on the area of the electron transport system between cytochrome c and oxygen.…”

Section: Action Of the Toxin On Mammalian Mitochondriamentioning

confidence: 99%