Studies on cytochrome aa3 of paracoccus dentrificans.

by Richard Turner

Publisher: University of East Anglia in Norwich

Written in English
Published: Downloads: 878
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Thesis (Ph.D), University of East Anglia, School of Biological Sciences, 1990.

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Open LibraryOL14592910M

  Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC ) was purified from the cytoplasmic membrane of the bacterium Paracoccus denitrificans. The enzyme contains two heme groups (a and a3) and two copper atoms per minimal unit, oxidizes mammalian cytochrome c at a high rate, and, when incorporated into liposomes, generates. The periplasmically located cytochrome c of Paracoccus denitrificans was purified from cells grown Duringaerobicgrowth, aa3- ando-type oxidases are formed (45). In a previous in vitro study byothers, it wassuggested that cytochrome Ci was . Studies in cytochrome aa3 of Paracoccus denitrificans. Author: Turner, Richard. ISNI: Awarding Body: University of East Anglia Current Institution: University of East Anglia Date of Award: Availability of Full Text: Access from EThOS.   By using synthetic oligonucleotides, the gene encoding soluble cytochrome c was isolated from a genomic bank of Paracoccus denitrificans. The nucleotide sequence of the gene was determined, and the deduced amino acid sequence of the mature protein was found to be similar to the primary structure of purified cytochrome c except for the.

Here we show that most of the optical spectral shift of native heme a is due to a hydrogen-bonding interaction between the formyl group and arginine in subunit I of cytochrome aa3 from Paracoccus denitrificans, and that a smaller part is due to an electrostatic interaction between the D ring propionate of heme a and arginine Structure at A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Ostermeier, C., Harrenga, A., Ermler, U., Michel, H. () Proc Natl Acad Sci U S A PubMed: Search on PubMed Search on PubMed Central; DOI: /pnasCited by: rial enzymes, the cytochrome c oxidase from Paracoccus denitrificans is particularly well suited as a model system (Ludwig, ). The P. denitrificans enzyme consists of three subunits that correspond to the three mitochondri- ally encoded subunits of the eukaryotic enzyme (subunits, I, 11, and ).Cited by: 5.   The crystal structure at Å resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment, is Cited by:

  Kleinschroth T, Castellani M, Trinh CH, Morgner N, Brutschy B, Ludwig B, Hunte C () X-ray structure of the dimeric cytochrome bc(1) complex from the soil bacterium Paracoccus denitrificans at A by: 1. Cytochrome c (PDB: C) in Paracoccus denitrificans. Created by: Keegan Krick The single-chain Cytochrome c found in Paracoccus denitrificans (PDB: C) is an integral periplasmic protein in the bacterial growth system across a host of physiological ically, the Cytochrome c protein transfers electrons between .   The cytochromebc 1 complex purified fromP. denitrificans has the same electron-transfer and energy-transducing activities, is sensitive to the same electron-transfer inhibitors, and contains cytochromesb, c 1, iron-sulfur protein, and thermodynamically stable ubisemiquinone identical to the counterpart complexes from mitochondria. However, the bacterialbc 1 complex Cited by:   Abstract. Several heme aa 3-type cytochrome c oxidases, purified from the cytoplasmic membranes of bacteria, are able to catalyze the same reactions as the structurally far more complex eukaryotic enzyme, i.e., electron transport from cytochrome c to oxygen coupled to proton translocation. However, these oxidases show a very simple subunit pattern, and Cited by:

Studies on cytochrome aa3 of paracoccus dentrificans. by Richard Turner Download PDF EPUB FB2

0 FEBS The Paracoccus denitrificans cytochrome aa3 has a third subunit. Tuomas HALTIA, Anne PUUSTINEN and Moshe FINEL. Department of Medical Chemistry, University of Helsinki.

(Received October S/Novem ) - EJB 87 The presence of a third polypeptide subunit in Paracoccus cytochrome c oxidase is by: Here we report that mutations of Glu56 or Gln63 in a newly described Ca2+/Na+ binding site in subunit I of cytochrome c oxidase from Paracoccus denitrificans [Ostermeier et al.

() Proc. Natl. Acad. Sci. U.S.A. 94, −] establish the Ca2+-dependent spectral shift in Cited by: Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the subunit beef heart enzyme Author links open overlay panel K. Pardhasaradhi B.

Ludwig R.W. HendlerCited by: Mutants deficient in the metabolism of one-carbon compounds have been obtained by treating Paracoccus denitrificans with the mutagen N-methyl-N'-nitro-N-nitrosoguanidine. The effect of a monoclonal antibody to a soluble cytochrome c from Paracoccus denitrificans was tested on the membrane-bound electron-transport system of this bacterium.

Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the subunit beef heart enzyme Pardhasaradhi, K. Abstract. Publication: Biophysical Journal. Pub Date: August DOI: /S(91)   Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC ) was purified from the cytoplasmic membrane of the bacterium Paracoccus denitrificans.

The enzyme contains two heme groups (a and a3) and two copper atoms per minimal unit, oxidizes mammalian cytochrome c at a high rate, and, when incorporated into liposomes, generates Cited by: A series of experiments are described in which mixtures of Paracoccus denitrificans, grown under denitrifying conditions, and cytochrome c′ purified from the same source were used to test whether cytochrome c′ is able to bind NO produced during by: The rebinding of CO to cytochrome c oxidase from Paracoccus denitrificans in the fully reduced and in the half-reduced (mixed valence) form as a function of temperature was investigated using time-resolved rapid-scan FT-IR spectroscopy in the mid-IR (− cm-1).

For the fully reduced enzyme, rebinding was complete in approximately 2 s at K and Cited by: Oxidation of compounds with one carbon atom. Paracoccus denitrificans can grow on methanol or methylamine as the sole carbon source.

The respective dehydrogenases (Figure ) are found in the periplasm. That for methanol contains pyrroloquinoline quinone (PQQ) as. G.J. Steffens and G. Buse, Studies on Cytochrome c Oxidase, IV; Primary Structure and Function of Subunit II, Hoppe- Seyler fs Z.

Physiol Chem. Google Scholar by: 7. Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the subunit beef heart enzyme. Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Cited by: Domain rotation of the Rieske iron–sulfur protein (ISP) between the cytochrome (cyt) b and cyt c 1 redox centers plays a key role in the mechanism of the cyt bc 1 complex.

Electron transfer within the cyt bc 1 complex of Paracoccus denitrificans was studied using a ruthenium dimer to rapidly photo-oxidize cyt c 1 within 1 μs and initiate the reaction.

In the absence of any added Cited by: 7. The two-subunit cytochrome c oxidase from Paracoccus denitrificans has been sequentially digested with chymotrypsin and Staphylococcus aureus V8 protease. The smaller subunit of the enzyme (apparent Mr 32,) was split into numerous peptides that were removed by anion-exchange by: preparation).

Cytochromeais alsopresentinmorethan oneform (Hendleret al., ; this paper). Inaddition to cooperative interactions between and among dif-ferentredoxcenters, themultiplicity ofmidpointpoten-tials can be attributed to different conformational and aggregationstatesoftheenzyme.

The mammalian cytochrome aa3 has 13 polypeptide. A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans. This article has been cited by other articles in PMC. Abstract. Cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, EC ) was purified from the cytoplasmic membrane of the bacterium Paracoccus by: 1.

Introduction. In aerobically grown Paracoccus denitrificans, the cytochrome bc 1 complex and the aa 3-type cytochrome oxidase have been shown to be arranged in a stoichiometric supercomplex and can be purified as such.Electron transfer between cyt c 1 and subunit II of the oxidase is mediated by a membrane-bound cytochrome c which is an integral part of Author: Gérard Lipowski, Ursula Liebl, Ursula Liebl, Bruno Guigliarelli, Wolfgang Nitschke, Barbara Schoepp.

Ludwig B, Schatz G. A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans. Proc Natl Acad Sci U S A. Jan; 77 (1)– [Europe PMC free article] [Google Scholar] Reddy KV, Hendler RW.

Complete analysis of the cytochrome components of beef heart mitochondria in terms of spectra and redox properties. To monitor the docking site for cytochrome c on cytochrome oxidase from Paracoccus denitrificans, a series of site‐directed mutants in acidic residues exposed on the three largest subunits was constructed, and the purified enzymes were assayed for their steady‐state kinetic parameters, their ionic strength dependence, and their fast electron entry Cited by: Previous work from this laboratory has revealed a complex and interactive redox behavior for the active metal centers in beef heart cytochrome aa3.

All of these centers are contained in two of the 13 subunits which make up the enzyme. The isolated cytochrome aa3 of Paracoccus denitrificans contains only two subunits. The purpose of the current investigation was to see Cited by: The studies show that the cytochromes c have multiple tasks in electron transfer.

The cytochrome bc 1 complex is the electron acceptor of the Q-pool and of amicyanin. It is also the electron donor to cytochromes c and c and to the cbb 3 -type by: The docking site for cytochrome c [14, 15] is located in subunit two, which contains the Cu A mixedvalence binuclear center with two Cu atoms separated by Å [16].

The Cu A site is the. Molecular Microbiology () 20(6), Structural and functional analysis of aa3-type and cbb3-type cytochrome c oxidases of Paracoccus denitrificans. This article is cited by 9 publications. Matthew W. Wolf, Kimberly Rizzolo, Sean J. Elliott, Nicolai Lehnert.

Resonance Raman, Electron Paramagnetic Resonance, and Magnetic Circular Dichroism Spectroscopic Investigation of Diheme Cytochrome c Peroxidases from Nitrosomonas europaea and Shewanella by: Cytochrome c expression in Paracoccus denitrificans strongly depends on growth condition: Identification of promoter region for cycA by transcription start analysis.

The periplasmic cytochrome c content of Paracoccus denitrificans has been shown by immunological detection to be strongly dependent on the mode of growth. Functional and structural studies on the Atmungsferment Cytochrome c oxidase from Paracoccus denitrificans.

Site-Directed Mutagenesis Studies on Subunit-I of the Aa3-Type Cytochrome-COxidase of Rhodobacter-Sphaeroides - a Brief Review of Progress to Date. The Paracoccus denitrificans cytochrome aa3 has a third : Heike Angerer.

The two-subunit cytochrome c oxidase from Paracoccus denitrificans contains two heme a groups and two copper atoms. However, when the enzyme is isolated from cells grown on a commonly employed medium, its electron paramagnetic resonance (EPR) spectrum reveals not only a Cu(II) powder pattern, but also a hyperfine pattern from tightly bound Mn(II).Cited by: The isolated cytochrome aa3 of Paracoccus denitrificans contains only two subunits.

The purpose of the current investigation was to see if the complex redox behavior is dependent on the presence of the additional 11 peptides that are present in the mammalian : K. Pardhasaradhi, B. Ludwig and R.W. Hendler. Synthetic oligonucleotide probes were used to clone two loci from the chromosomal DNA of Paracoccus denitrificans that contain the genes for cytochrome c oxidase (cytochrome aa 3).

One locus seems to contain four or five genes probably forming an operon. Two of these code for the oxidase subunits II and by: The structure of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase was investigated by perfusion-induced attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy.

Transitions from the oxidized to PM state were initiated by perfusion with CO/oxygen buffer, and the extent of conversion was quantitated by simultaneously monitoring Cited by:.

Aerobically grown Paracoccus denitrifcans ex- presses a mitochondrial-type respiratory chain [ 1,2]. The terminal catalyst is a cytochrome aa (3) which transfers electrons from cytochrome c to oxygen and couples this to proton translocation across the membrane.

The P. denitrificans cyt. aa has at least. In the accompanying paper, we have shown that the two-subunit cytochrome aa3 isolated from Paracoccus denitrificans displays the same kind of complex and interactive redox behavior as the subunit cytochrome aa3 from beef heart.

Therefore, the redox characteristics are not dependent on the additional 11 by: A two-subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus dentrificans plasmic membrane of the bacterium Paracoccus denitrificans.

The enzyme contains two heme groups (a and a3) and two cop- The present study was undert4ken in the hope that cyto.