Nomenclature Abstract for Paracoccus denitrificans (Beijerinck and Minkman 1910) Davis et al. 1969 (Approved Lists 1980) emend. Hördt et al. 2020.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Paracoccus Denitrificans

scholarly journals Paracoccus denitrificans: a genetically tractable model system for studying respiratory complex I

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Owen D. Jarman ◽  
Olivier Biner ◽  
John J. Wright ◽  
Judy Hirst
Keyword(s):  
Complex I ◽  
Paracoccus Denitrificans ◽  
Model System ◽  
Proton Pumping ◽  
Model Systems ◽  
Metabolic Enzyme ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Inner Mitochondrial Membrane

AbstractMitochondrial complex I (NADH:ubiquinone oxidoreductase) is a crucial metabolic enzyme that couples the free energy released from NADH oxidation and ubiquinone reduction to the translocation of four protons across the inner mitochondrial membrane, creating the proton motive force for ATP synthesis. The mechanism by which the energy is captured, and the mechanism and pathways of proton pumping, remain elusive despite recent advances in structural knowledge. Progress has been limited by a lack of model systems able to combine functional and structural analyses with targeted mutagenic interrogation throughout the entire complex. Here, we develop and present the α-proteobacterium Paracoccus denitrificans as a suitable bacterial model system for mitochondrial complex I. First, we develop a robust purification protocol to isolate highly active complex I by introducing a His6-tag on the Nqo5 subunit. Then, we optimize the reconstitution of the enzyme into liposomes, demonstrating its proton pumping activity. Finally, we develop a strain of P. denitrificans that is amenable to complex I mutagenesis and create a catalytically inactive variant of the enzyme. Our model provides new opportunities to disentangle the mechanism of complex I by combining mutagenesis in every subunit with established interrogative biophysical measurements on both the soluble and membrane bound enzymes.

scholarly journals Control of bacterial nitrate assimilation by stabilization of G-quadruplex DNA

2016 ◽  
Vol 52 (92) ◽  
pp. 13511-13514 ◽  
Author(s):  
Zoë A. E. Waller ◽  
Benjamin J. Pinchbeck ◽  
Bhovina Seewoodharry Buguth ◽  
Timothy G. Meadows ◽  
David J. Richardson ◽  
...  
Keyword(s):  
Promoter Region ◽  
Paracoccus Denitrificans ◽  
Nitrate Assimilation ◽  
Quadruplex Dna ◽  
G Quadruplex ◽  
Specific Control

Ligand-specific control of nitrate assimilation inParacoccus denitrificansby stabilization of DNA G-quadruplex in the promoter region ofnas.

Design and analysis of experiments on double substrate-limited growth of Paracoccus denitrificans

1984 ◽  
Vol 50 (1) ◽  
pp. 102-102
Author(s):  
E. D. Schoen ◽  
M. A. E. van der Heijden ◽  
H. W. van Verseveld ◽  
A. H. Stouthamer ◽  
J. C. Jager
Keyword(s):  
Paracoccus Denitrificans ◽  
Limited Growth ◽  
Double Substrate

Molybdenum incorporation in denitrifying Azospirillum brasilense Sp7

1992 ◽  
Vol 38 (10) ◽  
pp. 1042-1047 ◽  
Author(s):  
Christian Chauret ◽  
Wilfredo L. Barraquio ◽  
Roger Knowles
Keyword(s):  
Nitrate Reductase ◽  
Key Words ◽  
Nitrate Reduction ◽  
Gel Electrophoresis ◽  
Azospirillum Brasilense ◽  
Paracoccus Denitrificans ◽  
Free Medium ◽  
Azospirillum Brasilense Sp7

Nondenaturating disc gel electrophoresis revealed that 99Mo was incorporated into the nitrate reductase of Azospirillum brasilense grown in the absence but not in the presence of tungstate. Under denitrifying conditions, A. brasilense grown in tungsten-free medium steadily accumulated 99Mo for 12 h. In contrast, Paracoccus denitrificans grown under the same conditions ceased uptake after 1 h. However, both bacteria were incapable of accumulating significant amounts of 99Mo in media containing 10 mM tungstate, even though nitrate was reduced by A. brasilense. Aerobically grown A. brasilense cells transported 99Mo more efficiently than anaerobically grown cells. Key words: Azospirillum brasilense, tungsten, molybdenum incorporation, nitrate reduction.

scholarly journals Iron as a possible mediator of the oxic-to-anoxic transition in Paracoccus denitrificans

IUBMB Life ◽  
1997 ◽  
Vol 43 (2) ◽  
pp. 305-310
Author(s):  
Igor Kucera ◽  
Ivana Mat'chová
Keyword(s):  
Paracoccus Denitrificans
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