Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Marjaana Rönnberg"'
Publikováno v:
Biochimica et biophysica acta. 1080(1)
The secondary structure of Pseudomonas cytochrome c peroxidase (ferrocytochrome c : hydrogen-peroxide oxido-reductase, EC 1.11.1.5) has been predicted from the established amino acid sequence of the enzyme using a Chou-Fasman-type algorithm. The amou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a6d66c10a9219653a7d95a3875e0803
https://pubmed.ncbi.nlm.nih.gov/1657179
https://pubmed.ncbi.nlm.nih.gov/1657179
Autor:
Marjaana Rönnberg, Nils Ellfolk, Mona Grönlund, Anna-Britta Hörnfeldt, Rolf Servin, Hans Sternerup
Publikováno v:
Acta Chemica Scandinavica. :719-727
The steady state kinetics of cytochrome c peroxidase from Pseudomonas aeruginosa (PaCCP) has been studied by initial velocity techniques using several cytochromes c (550 and 555 P. aeruginosa; 551 P. fluorescens) and Pseudomonas azurin as electron do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d635df34a999f8ded5a84ac92a76cada
https://doi.org/10.3891/acta.chem.scand.29b-0719
https://doi.org/10.3891/acta.chem.scand.29b-0719
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 784:62-67
The anion-binding characteristics of resting and half-reduced Pseudomonas cytochrome c peroxidase (ferrocytochrome c-551: hydrogen peroxide oxidoreductase, EC 1.11.1.5) have been examined by EPR and optical spectroscopy with cyanide, azide and fluori
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9af459d2a85e533b644220cff48f90a5
https://doi.org/10.1016/0167-4838(84)90173-0
https://doi.org/10.1016/0167-4838(84)90173-0
Autor:
Marjaana Rönnberg
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 912:82-86
The amino acid sequences of the two heme c-containing tryptic peptides of Pseudomonas cytochrome-c peroxidase have been determined. The tryptic peptides were isolated from two cyanogen bromide fragments of the protein. Both heme-binding sites have th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97a9875e4a5e73a501b7434c06becef5
https://doi.org/10.1016/0167-4838(87)90250-0
https://doi.org/10.1016/0167-4838(87)90250-0
The reaction between reduced azurin and oxidized cytochrome c peroxidase from Pseudomonas aeruginosa
Publikováno v:
Journal of Biological Chemistry. 256:2471-2474
The reaction between ferric Pseudomonas cytochrome c peroxidase and reduced azurin was investigated by static titration, rapid scan, and stopped flow techniques as well as circular dichroism measurements. Kinetics of the reduction of the enzyme under
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ad4e83a45fc2cb274c1632861e9ae6f
https://doi.org/10.1016/s0021-9258(19)69805-4
https://doi.org/10.1016/s0021-9258(19)69805-4
Publikováno v:
FEBS Letters. 250:175-178
The primary structure of Pseudomonas cytochrome c peroxidase is presented. The intact protein was fragmented with cyanogen bromide into five fragments; partial cleavage was observed at a Met-His bond of the protein. The primary structure was establis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9adbc4daab3ab74fda98c8e002df1ef
https://doi.org/10.1016/0014-5793(89)80714-8
https://doi.org/10.1016/0014-5793(89)80714-8
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 828:67-72
The ferric-ferric (resting) form of Pseudomonas cytochrome c peroxidase will not bind cyanide. The half-reduced form binds cyanide to the ferric heme with a rate constant of (6.5 ± 0.2)·104 M−1·s−1 at pH 6, 25°C and ionic strength 0.1. The di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b4d05e79b48b1c029edcbeb310729161
https://doi.org/10.1016/0167-4838(85)90010-x
https://doi.org/10.1016/0167-4838(85)90010-x
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 791:9-14
The spin-states of the two c-type hemes in cytochrome c peroxidase from Pseudomonas aeruginosa have been investigated by 1H-NMR and magnetic susceptibility measurements. The susceptibility results indicate the presence of a low-spin high-spin equilib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bc3cf1970b8cee6ea5b22e06f2b6876
https://doi.org/10.1016/0167-4838(84)90274-7
https://doi.org/10.1016/0167-4838(84)90274-7
Autor:
Marjaana Rönnberg, Nils Ellfolk, H. Brian Dunford, Albert Dorfman, William B. Upholt, Curt R. Enzell
Publikováno v:
Acta Chemica Scandinavica. :79-83
The effect of pH on the stability and overall catalytic activity of half-reduced Pseudomonas cytochrome c peroxidase was studied over the pH range 3.5-8. The stability of the enzyme as deduced from 40 s incubation experiments is virtually unaffected
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4d9b4bdb9c68b8a91bfa9e5471417e8
https://doi.org/10.3891/acta.chem.scand.38b-0079
https://doi.org/10.3891/acta.chem.scand.38b-0079
Autor:
Gustav Schroll, L. Nørskov, Tuula Pakkanen, Gösta Brunow, Rolf Servin, Hans Sternerup, Marjaana Rönnberg, Lars-Göran Wistrand, Gerd Teien
Publikováno v:
Acta Chemica Scandinavica. :22-26
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0bc068c6a48762350dd58001d4c850b8
https://doi.org/10.3891/acta.chem.scand.33b-0022
https://doi.org/10.3891/acta.chem.scand.33b-0022