Energetic aspects of growth of Paracoccus denitrificans: oxygen-limitation and shift from anaerobic nitrate-limination to aerobic succinate-limitation - Evidence for a new alternative oxidase, cytochrome a1

H. W. van Verseveld, M. Braster, F. C. Boogerd, B. Chance, A.H. Stouthamer

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

1. Growth yields and efficiency of energy conservation were the same for aerobic succinate-limited and oxygen-limited cells of Paracoccus denitrificans. 2. A shift from anaerobic nitrate-limitation to aerobic succinatelimitation showed that before and after the shift cells grew with the same capacity of energy conservation. 3. Respiration-driven proton translocation showed the presence of H+-translocating sites 1 and 2, which translocate respectively 2-3 and 4 protons per 2 electrons in oxygen-, anaerobic nitrate-and aerobic succinate-limited cells. 4. Cytochrome spectra and flash-photolysis spectra of oxygen- and nitrate-limited cells gave evidence for the presence of an alternative oxidase, cytochrome a1, never before recognized in Paracoccus denitrificans. 5. Only a-type cytochromes liganded with CO could be flash-photolysed. No evidence for a functional cytochrome o was found in photolysis experiments. 6. Fast oxidation, before photolysis, of the bc-pool after introduction of oxygen in a CO-liganded sample at-20° to-30° C, indicated the presence of a cytochrome oxidase other than cytochrome a1 with a very high affinity for oxygen and a low affinity for CO. 7. In photochemical action spectra, light released CO-inhibition of respiration, but the release was independent of the wavelength used (560-610 nm).

Original languageEnglish
Pages (from-to)229-236
Number of pages8
JournalArchives of Microbiology
Volume135
Issue number3
DOIs
Publication statusPublished - Sep 1983

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Cytochromes a1
Paracoccus denitrificans
Succinic Acid
Nitrates
Carbon Monoxide
Oxygen
Photolysis
Cytochromes
Growth
Protons
Energy conservation
Respiration
Electron Transport Complex IV
alternative oxidase
Electrons
Light
Wavelength
Oxidation

Keywords

  • Chemostat
  • CO-Ligands
  • Cytochrome oxidase
  • Growth yields
  • Oxidative phosphorylation
  • Paracoccus denitrificans
  • Proton translocation

Cite this

@article{c62a4f9553b7422a9201cca696664872,
title = "Energetic aspects of growth of Paracoccus denitrificans: oxygen-limitation and shift from anaerobic nitrate-limination to aerobic succinate-limitation - Evidence for a new alternative oxidase, cytochrome a1",
abstract = "1. Growth yields and efficiency of energy conservation were the same for aerobic succinate-limited and oxygen-limited cells of Paracoccus denitrificans. 2. A shift from anaerobic nitrate-limitation to aerobic succinatelimitation showed that before and after the shift cells grew with the same capacity of energy conservation. 3. Respiration-driven proton translocation showed the presence of H+-translocating sites 1 and 2, which translocate respectively 2-3 and 4 protons per 2 electrons in oxygen-, anaerobic nitrate-and aerobic succinate-limited cells. 4. Cytochrome spectra and flash-photolysis spectra of oxygen- and nitrate-limited cells gave evidence for the presence of an alternative oxidase, cytochrome a1, never before recognized in Paracoccus denitrificans. 5. Only a-type cytochromes liganded with CO could be flash-photolysed. No evidence for a functional cytochrome o was found in photolysis experiments. 6. Fast oxidation, before photolysis, of the bc-pool after introduction of oxygen in a CO-liganded sample at-20° to-30° C, indicated the presence of a cytochrome oxidase other than cytochrome a1 with a very high affinity for oxygen and a low affinity for CO. 7. In photochemical action spectra, light released CO-inhibition of respiration, but the release was independent of the wavelength used (560-610 nm).",
keywords = "Chemostat, CO-Ligands, Cytochrome oxidase, Growth yields, Oxidative phosphorylation, Paracoccus denitrificans, Proton translocation",
author = "{van Verseveld}, {H. W.} and M. Braster and Boogerd, {F. C.} and B. Chance and A.H. Stouthamer",
year = "1983",
month = "9",
doi = "10.1007/BF00414485",
language = "English",
volume = "135",
pages = "229--236",
journal = "Archives of Microbiology",
issn = "0302-8933",
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Energetic aspects of growth of Paracoccus denitrificans : oxygen-limitation and shift from anaerobic nitrate-limination to aerobic succinate-limitation - Evidence for a new alternative oxidase, cytochrome a1. / van Verseveld, H. W.; Braster, M.; Boogerd, F. C.; Chance, B.; Stouthamer, A.H.

In: Archives of Microbiology, Vol. 135, No. 3, 09.1983, p. 229-236.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Energetic aspects of growth of Paracoccus denitrificans

T2 - oxygen-limitation and shift from anaerobic nitrate-limination to aerobic succinate-limitation - Evidence for a new alternative oxidase, cytochrome a1

AU - van Verseveld, H. W.

AU - Braster, M.

AU - Boogerd, F. C.

AU - Chance, B.

AU - Stouthamer, A.H.

PY - 1983/9

Y1 - 1983/9

N2 - 1. Growth yields and efficiency of energy conservation were the same for aerobic succinate-limited and oxygen-limited cells of Paracoccus denitrificans. 2. A shift from anaerobic nitrate-limitation to aerobic succinatelimitation showed that before and after the shift cells grew with the same capacity of energy conservation. 3. Respiration-driven proton translocation showed the presence of H+-translocating sites 1 and 2, which translocate respectively 2-3 and 4 protons per 2 electrons in oxygen-, anaerobic nitrate-and aerobic succinate-limited cells. 4. Cytochrome spectra and flash-photolysis spectra of oxygen- and nitrate-limited cells gave evidence for the presence of an alternative oxidase, cytochrome a1, never before recognized in Paracoccus denitrificans. 5. Only a-type cytochromes liganded with CO could be flash-photolysed. No evidence for a functional cytochrome o was found in photolysis experiments. 6. Fast oxidation, before photolysis, of the bc-pool after introduction of oxygen in a CO-liganded sample at-20° to-30° C, indicated the presence of a cytochrome oxidase other than cytochrome a1 with a very high affinity for oxygen and a low affinity for CO. 7. In photochemical action spectra, light released CO-inhibition of respiration, but the release was independent of the wavelength used (560-610 nm).

AB - 1. Growth yields and efficiency of energy conservation were the same for aerobic succinate-limited and oxygen-limited cells of Paracoccus denitrificans. 2. A shift from anaerobic nitrate-limitation to aerobic succinatelimitation showed that before and after the shift cells grew with the same capacity of energy conservation. 3. Respiration-driven proton translocation showed the presence of H+-translocating sites 1 and 2, which translocate respectively 2-3 and 4 protons per 2 electrons in oxygen-, anaerobic nitrate-and aerobic succinate-limited cells. 4. Cytochrome spectra and flash-photolysis spectra of oxygen- and nitrate-limited cells gave evidence for the presence of an alternative oxidase, cytochrome a1, never before recognized in Paracoccus denitrificans. 5. Only a-type cytochromes liganded with CO could be flash-photolysed. No evidence for a functional cytochrome o was found in photolysis experiments. 6. Fast oxidation, before photolysis, of the bc-pool after introduction of oxygen in a CO-liganded sample at-20° to-30° C, indicated the presence of a cytochrome oxidase other than cytochrome a1 with a very high affinity for oxygen and a low affinity for CO. 7. In photochemical action spectra, light released CO-inhibition of respiration, but the release was independent of the wavelength used (560-610 nm).

KW - Chemostat

KW - CO-Ligands

KW - Cytochrome oxidase

KW - Growth yields

KW - Oxidative phosphorylation

KW - Paracoccus denitrificans

KW - Proton translocation

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SN - 0302-8933

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