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2 edition of Characterisation of the NADH dehydrogenase from Paracoccus denitrificans found in the catalog.

Characterisation of the NADH dehydrogenase from Paracoccus denitrificans

Christina L. George

Characterisation of the NADH dehydrogenase from Paracoccus denitrificans

by Christina L. George

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Published by University of Birmingham in Birmingham .
Written in English


Edition Notes

Thesis (Ph.D.) - University of Birmingham, Dept of Biochemistry.

Statementby Christina L. George.
ID Numbers
Open LibraryOL13869886M

May 01,  · Analysis of the sequence homologies indicated that HndA shows 29, 21, and 26% identity with the kDa subunit from Bos taurus complex I, the kDa subunit from Paracoccus denitrificans NADH dehydrogenase type I, and the N-terminal domain of HoxF subunit of the NAD-reducing hydrogenase from Alcaligenes eutrophus, simplicityhsd.com by: Xu X, Matsuno-Yagi A, Yagi T. Structural features of the kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Arch Biochem Biophys. Jul; (1)– Yagi T. Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans. Arch Biochem Biophys.

The rate of NADH oxidation, catalysed by the inside‐out vesicles prepared from P. denitrificans cells increased up to 10 times on addition of uncouplers []. The electron flow within the bacterial complex I can be reversed by ΔµH + tightly coupled sub‐ Paracoccus particles (SPP) were shown to catalyse an efficient ΔµH + ‐dependent Cited by: Abstract. Membranes prepared from Haloferax denitrificans, Haloferax mediterranei and a Haloferax strain designated as Baja contained a nitrate reductase that was stable as well as most active in the absence of added NaCl (60 mM NaCl). Nitrate reduction was competitively inhibited by azide and chlorate; the latter also was a substrate. Cyanide inhibited the reduced form of the enzyme in an Cited by: 6.

Here, we report for the first time an infrared spectroscopic characterization of complex I. Electrochemically induced FT-IR difference spectra of complex I from Escherichia coli and of the NADH dehydrogenase fragment of this complex were obtained for critical potential simplicityhsd.com by: Isolation, sequencing, and mutagenesis of the gene encoding cytochrome ci of Paracoccus denitrificans and characterization of the mutant strain.


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Characterisation of the NADH dehydrogenase from Paracoccus denitrificans by Christina L. George Download PDF EPUB FB2

An NADH dehydrogenase complex was isolated from the plasma membranes of aerobically grown Paracoccus denitrificans cells by extraction with NaBr and purification on an NAD-agarose column. The NADH-ubiquinone-1 reductase activity of the isolated NADH dehydrogenase complex was about 10 times higher than that of the NaBr simplicityhsd.com by: Nov 01,  · Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans.

Yagi T. An NADH dehydrogenase complex was isolated from the plasma membranes of aerobically grown Paracoccus denitrificans cells by extraction with NaBr and purification on an NAD-agarose column.

The NADH-ubiquinone-1 reductase activity of the isolated NADH dehydrogenase Cited by: Using inverted membrane vesicles of P. denitrificans [ 1 ], this inhibition was shown to occur in the NADH dehydrogenase (EC ) region of the respiratory chain because, although respiration through segments II and III of the respiratory chain was unaffected by relatively high concentrations of the compound, it was markedly inhibited when NADH was used as the electron simplicityhsd.com by: Ferric reductase B (FerB) was initially isolated from Paraccoccus denitrificans as a homodimeric, FAD-containing flavoprotein capable of reducing various Fe(III) complexes with either NADH or, less efficiently, NADPH as the electron simplicityhsd.com by: The electron transport system of Paracoccus denitrificans (then known as Micrococcus denitrificans) first attracted significant interest in the ’s when it was shown that at least some of its components required for aerobic respiration are similar to those found in simplicityhsd.com by: 5.

Mar 08,  · Abstract. This study reports the expression of the flavoprotein (FP) subcomplex of the proton-translocating NADH-quinone oxidoreductase (NDH-1) from Paracoccus denitrificans, which is composed of the NQO1 (50 kDa) and the NQO2 (25 kDa) simplicityhsd.com two subunits are co-expressed in Escherichia coli using a double expression plasmid simplicityhsd.com by: Nov 29,  · Sulfite dehydrogenase activity was inhibited by sulfate and phosphate.

The structural and catalytic properties make sulfite dehydrogenase from P. denitrificans GB17 distinct from sulfite oxidases of other prokaryotic or eukaryotic simplicityhsd.com by: Sep 25,  · The F1FO and F1-ATPase complexes of Paracoccus denitrificans were isolated for the () Purification and characterization of NADH dehydrogenase complex from Paracoccus Harms, N., Hoogendijk, J., Stouthamer, A.

() Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and Cited by: Jan 01,  · 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 simplicityhsd.com by: Both insertions were mapped to min 51, and sequence analysis revealed that both mutated genes encode proteins homologous to subunits of mitochondrial NADH dehydrogenase I.

Crude extracts prepared from both mutant strains were able to oxidize NADH but lacked the enzymatic activity needed to oxidize deamino-NADH, a substrate specific for NADH dehydrogenase simplicityhsd.com by: Paracoccus denitrificans is a strictly respiring bacterium with a core respiratory chain similar to that of mammalian mitochondria.

As such, it continuously produces and has to cope with superoxide and other reactive oxygen species. In this work, the effects of artificially imposed superoxide stress on electron transport were simplicityhsd.com: Vojtěch Sedláček, Igor Kučera.

How- ever, the rate of electron transfer through all three segments (using NADH as electron donor) was markedly inhibited (Fig.

4a), indicating that Tinopal AN was a selective inhibitor of respiration in the NADH dehydrogenase region of the aerobic respiratory chain of P. simplicityhsd.com by: 9. EPR characterization of the iron-sulfur clusters in the NADH: ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans.

denitrificans NADH Dehydrogenase. Jun 15,  · Monospecific antibody to the respiratory NADH dehydrogenase from Paracoccus denitrificans was prepared by using as antigen specific immunoprecipitates containing NADH dehydrogenase which were excised from crossed-immunoelectrophoresis plates.

The latter were run with selectively solubilized plasma membranes and antibodies against plasma simplicityhsd.com by: 6. Reverse electron transfer, the process by which electrons from the reduced ubiquinol pool (supplied by succinate dehydrogenase, glycerolphosphate dehydrogenase, electron-transferring flavoprotein or dihydroorotate dehydrogenase in mammalian mitochondria) pass through complex I to reduce NAD + to NADH, driven by the inner mitochondrial membrane potential electric simplicityhsd.comnome: Isolation and characterization of complex I, rotenone‐sensitive NADH:ubiquinone oxidoreductase, from the procyclic forms of Trypanosoma brucei Author: Subject: DNA, NADH dehydrogenase, Paracoccus denitrificans, Trypanosoma brucei brucei, antibodies, antimycin A, capsaicin, Cited by: Paracoccus denitrificans is a strictly respiring bacterium with a core respiratory chain similar to that of mammalian mitochondria.

As such, it continuously produces and has to cope with. Characterisation of Membrane Vesicles from Paracoccus denitrificans and Measurements of the Effect of Partial Uncoupling on Their Thermodynamics of Oxidative Phosphorylation Article ·.

The respiratory nitrate reductase from Paracoccus denitrificans Molecular characterisation and kinetic properties to couple the oxidation of NADH to the production of duroquinol whtch acted as electron donor to nitrate The nitrate reductase system from P. denitrificans is Cited by: Nov 01,  · Abstract.

NADH dehydrogenase is the first component of the respiratory chain. It transfers electrons from NADH to ubiquinone and concomitantly establishes a proton motive force across the membrane. Salmonella typhimurium mutants defective in this enzyme were isolated in a screen for strains with increased expression of beta-galactosidase Cited by:.

A NADH dehydrogenase was isolated from an inner membrane-enriched fraction of beetroot mitochondria (Beta vulgaris L.) by solubilization with sodium deoxycholate and purified using gel filtration and affinity chromatography. The NADH dehydrogenase preparation contained a minor ATPase simplicityhsd.com by: Abstract.

Paracoccus denitrificans was grown aerobically in chemostat culture in the presence of rotenone. After 6 to 10 generation times, cells showed an oxygen uptake which was completely rotenone-insensitive after removal of rotenone by washing with bovine serum albumin containing simplicityhsd.com by: NADH dehydrogenase (ubiquinone) Synonyms.

13 kDa differentiation-associated protein. AMAPOR [49] CDA internal NADH dehydrogenase. NADH coenzyme Q1 reductase. NADH-CoQ oxidoreductase. NADH-CoQ reductase. ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans.

J. Biol.