The Experts below are selected from a list of 177 Experts worldwide ranked by ideXlab platform
Stuart J Ferguson - One of the best experts on this subject based on the ideXlab platform.
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The cytochromes c-550 of Paracoccus denitrificans and Thiosphaera pantotropha : a need for re-evaluation of the history of Paracoccus cultures
FEMS Microbiology Letters, 1996Co-Authors: Celia F. Goodhew, Stuart J Ferguson, Graham W. Pettigrew, Rob J.m. Van Spanning, Bart Devreese, Jozef Van Beeumen, Simon C. Baker, Neil F. W. Saunders, Ian P. ThompsonAbstract:The c-type cytochrome and protein profiles were compared for a number of cultures of Paracoccus denitrificans obtained from a range of culture collections. The cultures fell into two groups corresponding to the two original isolates of this bacterial species. One group, which included NCIMB 8944, ATCC 13543, ATCC 17741, ATCC 19367, Pd 1222 and DSM 413, were similar or identical to LMD 22.21. The second group, including DSM 65 and LMG 4218, were similar or identical to LMD 52.44. These groupings were not compatible with the recorded history of culture deposition. Mass spectrometry and amino acid sequence comparisons showed that the cytochrome c-550 of the LMD 52.44 culture group differed by 16% from that of the LMD 22.21 group, and yet was only 1% different from the cytochrome c-550 of Thiosphaera pantotropha. These results suggest that consideration should be given to creation of a new species of Paracoccus pantotropha, which would include Thiosphaera pantotropha and Paracoccus denitrificans LMD 52.44.
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The identification of a periplasmic nitrate reductase in Paracoccus denitrificans
FEMS Microbiology Letters, 1993Co-Authors: Heather J. Sears, Stuart J Ferguson, David J. Richardson, Stephen SpiroAbstract:A nitrate reductase activity has been identified in periplasmic extracts of Paracoccus denitrificans. The enzyme is relatively insensitive to azide and does not reduce chlorate, features which distinguish it from the well-characterised membrane-associated nitrate reductase. The specific activity of the enzyme was higher in intact cells grown with butyrate rather than succinate as the sole source of carbon.
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The functions and synthesis of bacterial c-type cytochromes with particular reference to Paracoccus denitrificans and Rhodobacter capsulatus.
Biochimica et Biophysica Acta, 1991Co-Authors: Stuart J FergusonAbstract:The properties of the c-type cytochromes are examined with special reference to their functional value in Paracoccus denitrificans and Rhodobacter capsulatus.
Judith P. Armitage - One of the best experts on this subject based on the ideXlab platform.
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inducible expression plasmid for rhodobacter sphaeroides and Paracoccus denitrificans
Applied and Environmental Microbiology, 2009Co-Authors: Alice C. Ind, Steven L. Porter, Mostyn T. Brown, Elaine D. Byles, Jennifer A. De Beyer, Scott A. Godfrey, Judith P. ArmitageAbstract:We have developed a stable isopropyl-beta-d-thiogalactopyranoside (IPTG)-inducible-expression plasmid, pIND4, which allows graduated levels of protein expression in the alphaproteobacteria Rhodobacter sphaeroides and Paracoccus denitrificans. pIND4 confers kanamycin resistance and combines the stable replicon of pMG160 with the lacI(q) gene from pYanni3 and the lac promoter, P(A1/04/03), from pJBA24.
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Inducible-expression plasmid for Rhodobacter sphaeroides and Paracoccus denitrificans.
Applied and environmental microbiology, 2009Co-Authors: Alice C. Ind, Steven L. Porter, Mostyn T. Brown, Elaine D. Byles, Jennifer A. De Beyer, Scott A. Godfrey, Judith P. ArmitageAbstract:We have developed a stable isopropyl-β-d-thiogalactopyranoside (IPTG)-inducible-expression plasmid, pIND4, which allows graduated levels of protein expression in the alphaproteobacteria Rhodobacter sphaeroides and Paracoccus denitrificans. pIND4 confers kanamycin resistance and combines the stable replicon of pMG160 with the lacIq gene from pYanni3 and the lac promoter, PA1/04/03, from pJBA24.
Rob J.m. Van Spanning - One of the best experts on this subject based on the ideXlab platform.
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Coping with formaldehyde during C1 metabolism of Paracoccus denitrificans.
Journal of Molecular Catalysis B-enzymatic, 2000Co-Authors: Rob J.m. Van Spanning, Simon De Vries, N. HarmsAbstract:Methylotrophic bacteria are capable of growth using reduced one-carbon (C1) compounds like methanol or methylamine as free energy sources. Paracoccus denitrificans, which is a facultative methylotrophic organism, switches to this type of autotrophic metabolism only when it experiences a shortage of available heterotrophic free energy sources. Since the oxidation of C1 substrates is energetically less favourable than that of the heterotrophic ones, a global regulatory circuit ensures that the enzymes involved in methylotrophic growth are repressed during heterotrophic growth. Once the decision is made to switch to methylotrophic growth, additional regulatory proteins ensure the fine-tuned expression of the participating enzymes such that the steady-state concentration of formaldehyde, the oxidation product of C1 substrates, is kept below cytotoxic levels. Copyright (C) 2000 Elsevier Science B.V.
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The cytochromes c-550 of Paracoccus denitrificans and Thiosphaera pantotropha : a need for re-evaluation of the history of Paracoccus cultures
FEMS Microbiology Letters, 1996Co-Authors: Celia F. Goodhew, Stuart J Ferguson, Graham W. Pettigrew, Rob J.m. Van Spanning, Bart Devreese, Jozef Van Beeumen, Simon C. Baker, Neil F. W. Saunders, Ian P. ThompsonAbstract:The c-type cytochrome and protein profiles were compared for a number of cultures of Paracoccus denitrificans obtained from a range of culture collections. The cultures fell into two groups corresponding to the two original isolates of this bacterial species. One group, which included NCIMB 8944, ATCC 13543, ATCC 17741, ATCC 19367, Pd 1222 and DSM 413, were similar or identical to LMD 22.21. The second group, including DSM 65 and LMG 4218, were similar or identical to LMD 52.44. These groupings were not compatible with the recorded history of culture deposition. Mass spectrometry and amino acid sequence comparisons showed that the cytochrome c-550 of the LMD 52.44 culture group differed by 16% from that of the LMD 22.21 group, and yet was only 1% different from the cytochrome c-550 of Thiosphaera pantotropha. These results suggest that consideration should be given to creation of a new species of Paracoccus pantotropha, which would include Thiosphaera pantotropha and Paracoccus denitrificans LMD 52.44.
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The terminal oxidases of Paracoccus denitrificans
Molecular microbiology, 1994Co-Authors: Jan-willem L. De Gier, Adriaan H. Stouthamer, Mathias Lübben, Willem Reijnders, Corinne A. Tipker, Dirk Jan Slotboom, Rob J.m. Van Spanning, John Van Der OostAbstract:Three distinct types of terminal oxidases participate in the aerobic respiratory pathways of Paracoccus denitrificans. Two alternative genes encoding subunit I of the aa3-type cytochrome c oxidase have been isolated before, namely ctaDI and ctaDII. Each of these genes can be expressed separately to complement a double mutant (delta ctaDI, delta ctaDII), indicating that they are isoforms of subunit I of the aa3-type oxidase. The genomic locus of a quinol oxidase has been isolated: cyoABC. This protohaem-containing oxidase, called cytochrome bb3, is the only quinol oxidase expressed under the conditions used. In a triple oxidase mutant (delta ctaDI, delta ctaDII, cyoB::KmR) an alternative cytochrome c oxidase has been characterized; this cbb3-type oxidase has been partially purified. Both cytochrome aa3 and cytochrome bb3 are redox-driven proton pumps. The proton-pumping capacity of cytochrome cbb3 has been analysed; arguments for and against the active transport of protons by this novel oxidase complex are discussed.
Bernd Ludwig - One of the best experts on this subject based on the ideXlab platform.
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structure at 2 8 a resolution of cytochrome c oxidase from Paracoccus denitrificans
Nature, 1995Co-Authors: So Iwata, Bernd Ludwig, Christian Ostermeier, Hartmut MichelAbstract:The crystal structure at 2.8 A resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a3-copper B binuclear centre where molecular oxygen is reduced to water. Two proton transfer pathways, one for protons consumed in water formation and one for 'proton pumping', could be identified. Mechanisms for proton pumping are discussed.
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Synthesis of the Rhodopseudomonas viridis holo-cytochrome c2 in Paracoccus denitrificans
FEMS microbiology letters, 1993Co-Authors: Ernst Gerhus, Bernd Ludwig, Hartmut Michel, Reinhard Grisshammer, Andreas TurbaAbstract:The gene encoding the Rhodopseudomonas viridis cytochrome c2(cycA) has been introduced on a broad host range vector into Paracoccus denitrificans, leading to high-level expression of the holo-cytochrome with the heme moiety covalently attached to the apoprotein. The cytochrome was demonstrated to reside in the periplasmic space of the host cell. In contrast to R. viridis, aerobic rather than anaerobic growth conditions led to higher production levels of the holo-cytochrome in P. denitrificans. This heterologous expression system provides a suitable genetic background for the functional expression and mutagenesis of polypeptides involved in bacterial photosynthesis, offering the possibility of detailed structural and functional investigation.
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Genetics of Paracoccus denitrificans.
FEMS microbiology reviews, 1993Co-Authors: P Steinrücke, Bernd LudwigAbstract:In bioenergetic research Paracoccus denitrificans has been used as an interesting model to elucidate the mechanisms of bacterial energy transduction. Genes for protein complexes of the respiratory chain and for proteins which are involved in periplasmic electron transport have been cloned and sequenced. Conjugational gene transfer has allowed the construction of site-specific mutant strains. Complementation experiments did not only open the field for site-directed mutagenesis and investigation of the structure/function relationship of the various electron-transport proteins, but also allowed first insights into processes like oxygen-dependent gene regulation or the assembly of electron-transport complexes. Also data will be presented that characterize two restriction-/modification systems, the codon usage and the promoter sequences of Paracoccus. Details will be given about the extrachromosomal localization of a duplicated cytochrome oxidase subunit I gene on one of the Paracoccus megaplasmids.
Hartmut Michel - One of the best experts on this subject based on the ideXlab platform.
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structure at 2 8 a resolution of cytochrome c oxidase from Paracoccus denitrificans
Nature, 1995Co-Authors: So Iwata, Bernd Ludwig, Christian Ostermeier, Hartmut MichelAbstract:The crystal structure at 2.8 A resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a3-copper B binuclear centre where molecular oxygen is reduced to water. Two proton transfer pathways, one for protons consumed in water formation and one for 'proton pumping', could be identified. Mechanisms for proton pumping are discussed.
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Synthesis of the Rhodopseudomonas viridis holo-cytochrome c2 in Paracoccus denitrificans
FEMS microbiology letters, 1993Co-Authors: Ernst Gerhus, Bernd Ludwig, Hartmut Michel, Reinhard Grisshammer, Andreas TurbaAbstract:The gene encoding the Rhodopseudomonas viridis cytochrome c2(cycA) has been introduced on a broad host range vector into Paracoccus denitrificans, leading to high-level expression of the holo-cytochrome with the heme moiety covalently attached to the apoprotein. The cytochrome was demonstrated to reside in the periplasmic space of the host cell. In contrast to R. viridis, aerobic rather than anaerobic growth conditions led to higher production levels of the holo-cytochrome in P. denitrificans. This heterologous expression system provides a suitable genetic background for the functional expression and mutagenesis of polypeptides involved in bacterial photosynthesis, offering the possibility of detailed structural and functional investigation.
