Oxidation of methylamine by a Paracoccus denitrificans mutant impaired in the synthesis of the bc1 complex and the aa3‐type oxidase Evidence for the existence of an alternative cytochrome c oxidase in this bacterium

Gier, J.-W. L. De; Spanning, Rob J.M. van; Oltmann, L. F.; Stouthamer, A. H.

doi:10.1016/0014-5793(92)80829-6

Cited by 14 publications

(13 citation statements)

References 12 publications

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“…The suspensions were incubated with succinate as reductant to the cytochromes, the reduction level of which was recorded spectrophotometrically in time (results not shown). Oxygen was supplied to these suspensions at a concentration of 1 mM by adding hydrogen peroxide, which is rapidly converted into oxygen and water by intracellular catalase activity (12). The traces show that the cytochromes c became more oxidized upon the addition of oxygen and became reduced again after oxygen had been fully consumed.…”

Section: Resultsmentioning

confidence: 99%

Cytochromes c ₅₅₀ , c ₅₅₂ , and c ₁ in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?

Otten

Oost²,

Reijnders³

et al. 2001

J Bacteriol

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Paracoccus denitrificans strains with mutations in the genes encoding the cytochrome c 550 , c 552 , or c 1 and in combinations of these genes were constructed, and their growth characteristics were determined. Each mutant was able to grow heterotrophically with succinate as the carbon and free-energy source, although their specific growth rates and maximum cell numbers fell variably behind those of the wild type. Maximum cell numbers and rates of growth were also reduced when these strains were grown with methylamine as the sole free-energy source, with the triple cytochrome c mutant failing to grow on this substrate. Under anaerobic conditions in the presence of nitrate, none of the mutant strains lacking the cytochrome bc 1 complex reduced nitrite, which is cytotoxic and accumulated in the medium. The cytochrome c 550 -deficient mutant did denitrify provided copper was present. The cytochrome c 552 mutation had no apparent effect on the denitrifying potential of the mutant cells. The studies show that the cytochromes c have multiple tasks in electron transfer. The cytochrome bc 1 complex is the electron acceptor of the Q-pool and of amicyanin. It is also the electron donor to cytochromes c 550 and c 552 and to the cbb 3 -type oxidase. Cytochrome c 552 is an electron acceptor both of the cytochrome bc 1 complex and of amicyanin, as well as a dedicated electron donor to the aa 3 -type oxidase. Cytochrome c 550 can accept electrons from the cytochrome bc 1 complex and from amicyanin, whereas it is also the electron donor to both cytochrome c oxidases and to at least the nitrite reductase during denitrification. Deletion of the c-type cytochromes also affected the concentrations of remaining cytochromes c, suggesting that the organism is plastic in that it adjusts its infrastructure in response to signals derived from changed electron transfer routes.

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Section: Resultsmentioning

confidence: 99%

Cytochromes c ₅₅₀ , c ₅₅₂ , and c ₁ in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?

Otten

Oost²,

Reijnders³

et al. 2001

J Bacteriol

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“…The Aaa3/c I mutant can still grow on Ct substrates, suggesting the presence of an alternative cytochrome c oxidase (De Gier et al, 1992). A likely candidate has recently been described in P. denitrificans: cytochrome cbb3 .…”

Section: The Aerobic Respiratory Networkmentioning

confidence: 95%

“…It has been recognized before that a complex catabolic network is involved in methylotrophic growth of P. denitrificans. The components that participate in the oxidation of methylamine and methanol include redox proteins that are involved in the respiratory electron transfer to oxygen, as well as dehydrogenases that catalyze the stepwise conversion of C~ substrate to carbon dioxide De Gier et al, 1992. Except for the genes that encode the formate dehydrogenase complex, all structural genes of the components that participate in the Ct catabolism of P. denitrificans have been cloned (Table I).…”

Section: The Aerobic Respiratory Networkmentioning

confidence: 99%

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

Spanning

Boer

Reijnders

et al. 1995

J Bioenerg Biomembr

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General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 12 May 2018Journal of Bioenergetics and Biomembranes, Vol. 27, No. 5, 1995 Received May 29, 1995 Paracoccus denitrificans is a facultative anaerobic bacterium that has the capacity to adjust its metabolic infrastructure, quantitatively and/or qualitatively, to the prevailing growth condition. In this bacterium the relative activity of distinct catabolic pathways is subject to a hierarchical control. In the presence of oxygen the aerobic respiration, the most efficient way of electron transfer-linked phosphorylation, has priority. At high oxygen tensions P. denitrificans synthesizes an oxidase with a relatively low affinity for oxygen, whereas under oxygen limitation a high-affinity oxidase appears specifically induced. During anaerobiosis, the pathways with lower free energy-transducing efficiency are induced. In the presence of nitrate, the expression of a number of dehydrogenases ensures the continuation of oxidative pbosphorylation via denitrification. After identification of the structural components that are involved in both the aerobic and the anaerobic respiratory networks of P. denitrificans, the intriguing next challenge is to get insight in its regulation. Two transcription regulators have recently been demonstrated to be involved in the expression of a number of aerobic and/or anaerobic respiratory complexes in P. denitrificans. Understanding of the regulation machinery is beginning to emerge and promises much excitement in discovery.KEY WORDS: Respiratory network; multiple oxidases; denitrification; gene regulation; FNR; Paracoccus denitrificans; Escherichia coli. ~TRODUCTIONThe ultimate goal of living organisms is to contribute to a continued existence of their species by means of survival and reproduction. In unicellular organisms, the ability to survive depends on the cell's potential to adapt its metabolism to the available carbon and free-energy sources in its natural habitat, ensuring maintenance and growth. The more such an environment is subject to fluctuations in the supply of these substrates, the higher the demands that are made upon the potential of the cell to adjust its metabolic properties. A profound example of this flexibility is the process of bacterial respiration...

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“…This suggests direct participation of the cytochrome c pool in the methylamine respiratory chain ; moreover, processing of the TTQ group of MADH probably requires the presence of a peroxidase-like cytochrome c (Lidstrom and Chistoserdov, 1993;Van der Palen et al, unpublished results cytochromes that are specifically expressed during methylotrophic growth Van Spanning et al, 1991 a, b). Likewise, oxidation of methylamine still occurs in a mutant strain lacking the ua3type cytochrome-c oxidase (Willison et al, 1981 ;Harms et al, 1985), and in a mutant devoid of both the bc, complex and the aa,-type oxidase (De Gier et al, 1992). These observations suggest the existence of alternative pathways of methylamine oxidation, branching at the level of amicyanin and/or cytochrome c. P. denitrificans possesses at least 12 different cytochrome c species (Bosma, 1989;Harms and Van Spanning, 1991).…”

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confidence: 99%

The Oxidation of Methylamine in Paracoccus denitrificans

Gier

Oost

Harms

et al. 1995

European Journal of Biochemistry

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The in vivo oxidation of methylamine has been studied in Paracoccus denitrificans. Four components are involved in the electron transfer from methylamine to oxygen; methylamine dehydrogenase (MADH), amicyanin, cytochrome c and cytochrome-c oxidase. In P. denitrificans, MADH and its electron acceptor amicyanin are indispensable for growth on methylamine. In the present study, site-directed mutants have been used to demonstrate participation of cytochrome c550 and the aa3-type cytochrome-c oxidase. Moreover, evidence is provided for the operation of alternative routes, branching from amicyanin, in which at least cytochrome c1 and the cbb3-type cytochrome-c oxidase are involved.

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Oxidation of methylamine by a Paracoccus denitrificans mutant impaired in the synthesis of the bc₁ complex and the aa₃‐type oxidase Evidence for the existence of an alternative cytochrome c oxidase in this bacterium

Cited by 14 publications

References 12 publications

Cytochromes c ₅₅₀ , c ₅₅₂ , and c ₁ in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?

Cytochromes c ₅₅₀ , c ₅₅₂ , and c ₁ in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

The Oxidation of Methylamine in Paracoccus denitrificans

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Oxidation of methylamine by a Paracoccus denitrificans mutant impaired in the synthesis of the bc1 complex and the aa3‐type oxidase Evidence for the existence of an alternative cytochrome c oxidase in this bacterium

Cited by 14 publications

References 12 publications

Cytochromes c 550 , c 552 , and c 1 in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?

Cytochromes c 550 , c 552 , and c 1 in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?

Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans

The Oxidation of Methylamine in Paracoccus denitrificans

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Oxidation of methylamine by a Paracoccus denitrificans mutant impaired in the synthesis of the bc₁ complex and the aa₃‐type oxidase Evidence for the existence of an alternative cytochrome c oxidase in this bacterium

Cytochromes c ₅₅₀ , c ₅₅₂ , and c ₁ in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?

Cytochromes c ₅₅₀ , c ₅₅₂ , and c ₁ in the Electron Transport Network of Paracoccus denitrificans : Redundant or Subtly Different in Function?