Oxidative phosphorylation in fractionated bacterial systems

Kashket, Eva R.; Brodie, Arnold F.

doi:10.1016/0006-3002(63)91608-1

Cited by 72 publications

(24 citation statements)

References 44 publications

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“…This agreed with the observation by TIssIEREs et al (5), but not with that by KASHKET and BRODIE (32). Figure 2 shows the kind of phosphorus compounds found in the reaction The reaction mixtures were the same as given in Table 1.…”

Section: Oxidation and Phosphorylation By Eleven Bacterial Systemssupporting

confidence: 87%

“…cycloclastes, only naphthoquinones in M lysodeikticus and Brev. helvolum, and both quinones in E. coli and A, aerogenes, though the side-chain length of the quinones in some bacteria was found to differ from those described in the previous reports (12,32). In their mass spectra, main molecular peak was observed at m/e 716 in MM lysodeikticus and E. coli, and at rn/e 784 in Brev.…”

Section: Quinones In Bacteriamentioning

confidence: 61%

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Oxidative Phosphorylation in Bacteria

Watanuki

Ōishi

Aida

et al. 1972

J. Gen. Appl. Microbiol.

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Oxidative phosphorylation in particulate fractions of eleven bacteria was examined without adding any soluble factor. The bacteria examined which could oxidize both NADH and succinate were divided from their properties of phosphorylation into the following three groups ; (i) phosphorylation is scarcely coupled to the oxidation of both substrates,(ii) the P : 0 ratio in NADH oxidation is nearly equal to that in succinate oxidation, and (iii) the P : 0 ratio in NADH oxidation is lower than that in succinate oxidation. The bacteria whose P : 0 ratio in NADH oxidation is higher than that in succinate oxidation were not observed.In small particles of strains from group (ii) 0.1 m1Vi of cyanide inhibited NADH and succinate oxidation at a similar rate, while in small particles of strains from group (iii) cyanide inhibited succinate oxidation more strongly than NADH oxidation.These groups agree well with the groups classified by the quinones present. The bacteria in group (ii) contain benzoquinones alone or, at least, mainly, and those in group (iii) contain naphthoquinones alone. From these observations, the role of quinones in oxidative phosphorylation of bacterial particles was discussed.

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Section: Oxidation and Phosphorylation By Eleven Bacterial Systemssupporting

confidence: 87%

Section: Quinones In Bacteriamentioning

confidence: 61%

Oxidative Phosphorylation in Bacteria

Watanuki

Ōishi

Aida

et al. 1972

J. Gen. Appl. Microbiol.

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“…Expt (B): the bacteria were grown up to the end of the exponential phase in 0. 5 Table 3. Distribution of respiratory components in fractions of P. rettgeri prepared by various methods The bacteria (Expts A and B) were grown up to the end of the exponential phase in 0.5 1 of the complex medium in shaken Fernbach flasks.…”

Section: Localization Of Q and M Kmentioning

confidence: 99%

“…Kashkett and Brodie [4,5] failed to restore the respixatory activity of E.coli by addition of quinones to preparations which had been inactivated by irradiation. Only the cytochrome c reduction with NADH and succinate could be reactivated.…”

Section: The Differential Roles Of Q and M K In Electron Transportmentioning

confidence: 99%

On the Role of Quinones in Bacterial Electron Transport

Kröger¹,

Dadák

Klingenberg³

et al. 1971

European Journal of Biochemistry

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The individual roles of ubiquinone and menaquinone in the electron transport of Proteus rettgeri have been investigated and their functional positions with respect to the cytochromes and dehydrogenases elucidated.1. A method has been developed for the parallel determination of both ubiquinone and menaquinone in the nanomole range in the same extract.2. Ubiquinone and menaquinone are not separated by various methods of cell disintegration and remain associated with the cytochromes.3. The relative contents of ubiquinone and menaquinone are independent of the hydrogen source and depend on the redox acceptor offered in the growth medium. As in Escherichia coli, ubiquinone is preferentially formed in cutures with maximal oxygen supply and menaquinone in anaerobic cultures. The activity offurnarate reduction by NADH and by formate parallels the content of menaquinone. 4.On extraction of the quinones the electron transport is inhibited. Ubiquinone reactivates the respiration with succinate, NADH and formate and menaquinone restores the fumarate reduction. I n anaerobically grown P . rettgeri the respiration with NADH and formate is partly restored by menaquinone, too.5. In the anaerobic states, ubiquinone is reduced with succinate, NADH and formate, and menaquinone with NADH and formate only. Ubiquinone is partly oxidized in the steady state of respiration and completely reduced in the steady state of fumarate reduction, where menaquinone is partly oxidized.6. 2-n-Heptyl-4-hydroxyquinoline-N-oxide inhibits the respiration of succinate, NADH and formate a t a common site located on the oxygen side of ubiquinone.7. Two b-type cytochromes (besides cytochrome 0) are differentialed: (1) Cytochrome b B is situated on the substrate side of 2-n-heptyl-4-hydroxyquinoline-N-oxide action and is reduced by formate only. (2) Cytochrome b1 is located on the oxygen side of this action and is reducible by all substrates.I n a previous communication [l] the role of the naphthoquinone derivative, menaquinone, was studied in a gram-positive organism (Bacillus megaterium) where it is the only occurring quinone. A basically similar role in the electron transport was attributed to menaquinone (MK) as to ubiquinone (Q) in mitochondria. A more penetrating insight into the particular role of both quinones and their differences is expected to be gained from the study of an organism where both quinones occur together, such as in the entero-bacteria, Escherichia and Proteus [2,3]. Different roles for Q and MK can be expected from the considerable differences or their redox potentials (see Discussion).Unusual Abbreviations. Ubiquinone, Q ; oxidized ubiquinone, Qox ; reduced ubiquinone, Qred ; menaquinone (vitamin K2), MK; oxidized menaquinone, MK,,; reduced menaquinone, =red.It is generally assumed that both quinones interact in the electron transport system of these organisms [4-91 although no redox reactions of MK have been demonstrated so far. Furthermore, the individual roles as reported in the literature have not been understood so far [lo-12...

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“…Nitrobacter agilis [6], Nitrobacter winogradskii [7]) yield respiratory membranes with highly efficient, self contained oxidative phosphorylation systems (P/O ratios up to 2.8 with NADH), whereas the heterotrophs (e. g . Escherichia coli [8,9]. Alcaligenes fuecalis [lo] and Azotobacter vinelandii [ l l , 121) in general yield respiratory membranes of much lower phosphorylation efficiency (P/O ratios with NADH rarely exceed 0.5), even when optimally supplemented with soluble factors.…”

Section: Mycobacterium Phlei [2] Corynebacterium Creatovoransmentioning

confidence: 99%

The Respiratory System of Azotobacter vinelandii

Ackrell¹,

Jones²

1971

European Journal of Biochemistry

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1. A detailed procedure is described for the isolation of stable respiratory membranes of relatively high phosphorylation efficiency from nitrogen-fixing cultures of Azotobacter vinelandii 2 . Three phosphorylation sites are detectable. These are located a t the level of NADH dehydrogenase (Site I; P/2e 0.45)) between the primary dehydrogenases and the cytochromes (Site 11; P/2e 0.53) and on the minor terminal pathway, to the oxygen side of the c-type cytochromes (Site 111; P/2e 0.22).3. Switching of electron flow between the terminal oxidation pathways with low concentrations of KCN and 2-n-alkyl-4-hydroxyquinoline-N-oxide causes changes in oxygen uptake and phosphate esterification which are compatible with the postulated locations of the three phosphorylation sites and which demonstrate, indirectly, the non-phosphorylating nature of the b, --f a2 major terminal pathway.4. Phosphorylation efficiences with ascorbate plus purified A . vinehndii cytochromes c4 and c5, horse heart cytochrome c and the artificial electron mediators 2,6-dichlorophenol indophenol and N,N,N',N'-tetramethyl-p-phenylene diamine indicate that the minor terminal pathway is further split into a slow, phosphorylating pathway (c5 --f oxygen) and a faster, non-phosphorylating pathway (c4 -+ oxygen).(P/O, NADH = 0.90-1.10).The efficiencies of oxidative phosphorylation exhibited by isolated bacterial respiratory membranes are in general very much lower than those of intact mammalian mitochondria [l].Cell free extracts of gram positive bacteria (e. g. Mycobacterium phlei [2], Corynebacterium creatovorans[3] and Micrococcus lysodeikticzcs [4]) exhibit high P/O ratios (up to 1.8 when oxidising succinate or malate, but lower with NADH) ; isolated respiratory membranes are less efficient, but can be stimulated to yield higher P/O ratios by the addition of soluble factors [2,4,5]. Of the gram negative bacteria so far studied, the chemoautotrophs (e. g . Nitrobacter agilis [6], Nitrobacter winogradskii [7]) yield respiratory membranes with highly efficient, self contained oxidative phosphorylation systems (P/O ratios up to 2.8 with NADH), whereas the heterotrophs (e. g . Escherichia coli [8,9]. Alcaligenes fuecalis [lo] and Azotobacter vinelandii [ l l , 121) in general yield respiratory membranes of much lower phosphorylation efficiency (P/O ratios with NADH rarely exceed 0.5), even when optimally supplemented with soluble factors.Definition. A,,, unit, the quantity af material contained in i m l of a solution which has an absorbance of i a t 680 nm when measured in a i-cm path length cell.The membrane-bound respiratory system of Azotobucter vinehndii is characterised by extremely high oxidase activities, particularly with NADH or malate, a rich and varied content of electron carriers and a branched terminal cytochrome system [13-161. The nature of this branched cytochrome system was elucidated via kinetic and inhibitor studies which suggested that the major electron flow was catalysed by cytochromes bl and a2 (sensitive to 2-n-alkyl-4-hydroxyquinol...

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Oxidative phosphorylation in fractionated bacterial systems

Cited by 72 publications

References 44 publications

Oxidative Phosphorylation in Bacteria

Oxidative Phosphorylation in Bacteria

On the Role of Quinones in Bacterial Electron Transport

The Respiratory System of Azotobacter vinelandii

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