Nomenclature Abstract for Paracoccus pantotrophus (Robertson and Kuenen 1984) Rainey et al. 1999 emend. Hördt et al. 2020.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Sarah Wigley ◽  
George M Garrity
Keyword(s):  
Paracoccus Pantotrophus

Voltammetric characterization of the aerobic energy-dissipating nitrate reductase of Paracoccus pantotrophus: exploring the activity of a redox-balancing enzyme as a function of electrochemical potential

2007 ◽  
Vol 409 (1) ◽  
pp. 159-168 ◽  
Author(s):  
Andrew J. Gates ◽  
David J. Richardson ◽  
Julea N. Butt
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Reductase Activity ◽  
Electrochemical Potential ◽  
Intact Cells ◽  
Protein Film ◽  
Protein Film Voltammetry ◽  
Voltammetric Studies ◽  
Paracoccus Pantotrophus

Paracoccus pantotrophus expresses two nitrate reductases associated with respiratory electron transport, termed NapABC and NarGHI. Both enzymes derive electrons from ubiquinol to reduce nitrate to nitrite. However, while NarGHI harnesses the energy of the quinol/nitrate couple to generate a transmembrane proton gradient, NapABC dissipates the energy associated with these reducing equivalents. In the present paper we explore the nitrate reductase activity of purified NapAB as a function of electrochemical potential, substrate concentration and pH using protein film voltammetry. Nitrate reduction by NapAB is shown to occur at potentials below approx. 0.1 V at pH 7. These are lower potentials than required for NarGH nitrate reduction. The potentials required for Nap nitrate reduction are also likely to require ubiquinol/ubiquinone ratios higher than are needed to activate the H+-pumping oxidases expressed during aerobic growth where Nap levels are maximal. Thus the operational potentials of P. pantotrophus NapAB are consistent with a productive role in redox balancing. A Michaelis constant (KM) of approx. 45 μM was determined for NapAB nitrate reduction at pH 7. This is in line with studies on intact cells where nitrate reduction by Nap was described by a Monod constant (KS) of less than 15 μM. The voltammetric studies also disclosed maximal NapAB activity in a narrow window of potential. This behaviour is resistant to change of pH, nitrate concentration and inhibitor concentration and its possible mechanistic origins are discussed.

Electrocatalytic reduction of nitrate and selenate by NapAB

2011 ◽  
Vol 39 (1) ◽  
pp. 236-242 ◽  
Author(s):  
Andrew J. Gates ◽  
Clive S. Butler ◽  
David J. Richardson ◽  
Julea N. Butt
Keyword(s):  
Cytoplasmic Membrane ◽  
Current Knowledge ◽  
Reductase Activity ◽  
Protonmotive Force ◽  
Metabolic Diversity ◽  
Protein Film ◽  
Carbon Substrates ◽  
Redox Poise ◽  
Paracoccus Pantotrophus ◽  
High Level

Bacterial cellular metabolism is renowned for its metabolic diversity and adaptability. However, certain environments present particular challenges. Aerobic metabolism of highly reduced carbon substrates by soil bacteria such as Paracoccus pantotrophus presents one such challenge since it may result in excessive electron delivery to the respiratory redox chain when compared with the availability of terminal oxidant, O2. The level of a periplasmic ubiquinol-dependent nitrate reductase, NAP, is up-regulated in the presence of highly reduced carbon substrates. NAP oxidizes ubiquinol at the periplasmic face of the cytoplasmic membrane and reduces nitrate in the periplasm. Thus its activity counteracts the accumulation of excess reducing equivalents in ubiquinol, thereby maintaining the redox poise of the ubiquinone/ubiquinol pool without contributing to the protonmotive force across the cytoplasmic membrane. Although P. pantotrophus NapAB shows a high level of substrate specificity towards nitrate, the enzyme has also been reported to reduce selenate in spectrophotometric solution assays. This transaction draws on our current knowledge concerning the bacterial respiratory nitrate reductases and extends the application of PFE (protein film electrochemistry) to resolve and quantify the selenate reductase activity of NapAB.

Hydrogen sulfide removal from biogas in biotrickling filter system inoculated with Paracoccus pantotrophus

2019 ◽  
Vol 44 (56) ◽  
pp. 29554-29560
Author(s):  
Jinjuta Juntranapaporn ◽  
Nunthaphan Vikromvarasiri ◽  
Cheema Soralump ◽  
Nipon Pisutpaisal
Keyword(s):  
Hydrogen Sulfide ◽  
Biotrickling Filter ◽  
Filter System ◽  
Sulfide Removal ◽  
Hydrogen Sulfide Removal ◽  
Paracoccus Pantotrophus

scholarly journals Draft Genome Sequences of the Nitrate-Dependent Iron-Oxidizing Proteobacteria Acidovorax sp. Strain BoFeN1 and Paracoccus pantotrophus Strain KS1

2018 ◽  
Vol 7 (10) ◽  
Author(s):  
A. Price ◽  
M. C. Macey ◽  
J. Miot ◽  
K. Olsson-Francis
Keyword(s):  
Draft Genome ◽  
Genome Sequences ◽  
Content Type ◽  
Iron Oxidizing Bacteria ◽  
Paracoccus Pantotrophus

The draft genomes of the nitrate-dependent iron-oxidizing bacteria Acidovorax sp. strain BoFeN1 and Paracoccus pantotrophus strain KS1 are presented.

scholarly journals Recombinant Sox Enzymes from Paracoccus pantotrophus Degrade Hydrogen Sulfide, a Major Component of Oral Malodor

2017 ◽  
Vol 32 (1) ◽  
pp. 54-60 ◽  
Author(s):  
Atik Ramadhani ◽  
Miki Kawada-Matsuo ◽  
Hitoshi Komatsuzawa ◽  
Takahiko Oho
Keyword(s):  
Hydrogen Sulfide ◽  
Oral Malodor ◽  
Paracoccus Pantotrophus

scholarly journals Identification of a transposable genomic island of Paracoccus pantotrophus DSM 11072 by its transposition to a novel entrapment vector pMMB2

Microbiology ◽  
2006 ◽  
Vol 152 (4) ◽  
pp. 1063-1073 ◽  
Author(s):  
Malgorzata Mikosa ◽  
Marta Sochacka-Pietal ◽  
Jadwiga Baj ◽  
Dariusz Bartosik
Keyword(s):  
Genomic Island ◽  
Tricarboxylic Acid Cycle ◽  
Housekeeping Genes ◽  
Core Region ◽  
Lateral Transfer ◽  
Large Set ◽  
Bacterial Genomes ◽  
The Core ◽  
Chromosomal Origin ◽  
Paracoccus Pantotrophus

A novel shuttle entrapment vector, pMMB2, was used to identify a large transposable element, TnPpa1 (44·3 kb), of Paracoccus pantotrophus DSM 11072. TnPpa1 has a composite structure with divergently oriented copies of a cryptic transposon, Tn3434 (Tn3 family), located at both termini. The core region of the element contains a large set of putative genes, whose products show similarity to enzymes involved in central intermediary metabolism (e.g. tricarboxylic acid cycle or 2-methylcitrate cycle), transporters, transcriptional regulators and conserved proteins of unknown function. A 4·2 kb DNA segment of TnPpa1 is homologous to a region of chromosome cII of Rhodobacter sphaeroides 2.4.1, which exemplifies the mosaic structure of this element. TnPpa1 is bordered by 5 bp long directly repeated sequences and is located within a mega-sized replicon, pWKS5, in the DSM 11072 genome. Spontaneous inversion of the core region of TnPpa1 was detected in the host genome. Analysis of the distribution of TnPpa1 in three other strains of P. pantotrophus revealed that this element was present exclusively within DSM 11072, which suggests its relatively recent acquisition by lateral transfer. The identification of TnPpa1 (which may be considered a transposable genomic island) provides evidence for the transposition and lateral transfer of large DNA segments of chromosomal origin (carrying various housekeeping genes), which may have a great impact on the evolution of bacterial genomes.

scholarly journals Identification of ccdA inParacoccus pantotrophus GB17: Disruption ofccdA Causes Complete Deficiency inc-Type Cytochromes

2001 ◽  
Vol 183 (1) ◽  
pp. 257-263 ◽  
Author(s):  
Frank Bardischewsky ◽  
Cornelius G. Friedrich
Keyword(s):  
Sulfur Oxidation ◽  
Open Reading Frames ◽  
Redox Mediators ◽  
Transmembrane Helices ◽  
Wild Type ◽  
Structural Identity ◽  
Paracoccus Pantotrophus ◽  
Type Gene ◽  
Extension Analysis ◽  
Reading Frames

ABSTRACT A transposon Tn5-mob insertional mutant ofParacoccus pantotrophus GB17, strain TP43, was unable to oxidize thiosulfate aerobically or to reduce nitrite anaerobically, and the cellular yields were generally decreased by 11 to 20%. Strain TP43 was unable to form functional c-type cytochromes, as determined by difference spectroscopy and heme staining. However, formation of apocytochromes and their transport to the periplasm were not affected, as seen with SoxD, a c-type cytochrome associated with the periplasmic sulfite dehydrogenase homologue. The Tn5-mob-containing DNA region of strain TP43 was cloned into pSUP205 to produce pE18TP43. With the aid of pE18TP43 the corresponding wild-type gene region of 15 kb was isolated from a heterogenote recombinant to produce pEF15. Sequence analysis of 2.8 kb of the relevant region uncovered three open reading frames, designated ORFA, ccdA, and ORFB, with the latter being oriented divergently. ORFA and ccdA were constitutively cotranscribed as determined by primer extension analysis. In strain TP43 Tn5-mob was inserted into ccdA. The deduced ORFA product showed no similarity to any protein in databases. However, the ccdA gene product exhibited similarities to proteins assigned to different functions in bacteria, such as cytochrome c biogenesis. For these proteins at least six transmembrane helices are predicted with the potential to form a channel with two conserved cysteines. This structural identity suggests that these proteins transfer reducing equivalents from the cytoplasm to the periplasm and that the cysteines bring about this transfer to enable the various specific functions via specific redox mediators such as thioredoxins. CcdA of P. pantotrophus is 42% identical to a protein predicted by ORF2, and its location within thesox gene cluster coding for lithotrophic sulfur oxidation suggested a different function.

The sulfur-oxidizing enzyme system of paracoccus pantotrophus: proteins and reaction

2003 ◽  
Vol 96 (1) ◽  
pp. 66
Author(s):  
Cornelius G. Friedrich ◽  
Armin Quentmeier ◽  
Frank Bardischewsky ◽  
Dagmar Rother ◽  
Petra Hellwig ◽  
...  
Keyword(s):  
Enzyme System ◽  
Sulfur Oxidizing ◽  
Paracoccus Pantotrophus
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