Zobrazeno 1 - 10
of 96
pro vyhledávání: '"Nils Ellfolk"'
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. 581:1-14
Resonance Raman spectra are reported for native ferric cytochrome c peroxidase, its cyanide and fluoride compounds, those of the ferrous enzyme and its cyanide and carbonyl compounds, and the spectrum of the hydrogen peroxide compound, compound I. Ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de8d3534e9954360a9d491eda40ab7c9
https://doi.org/10.1016/0005-2795(79)90215-0
https://doi.org/10.1016/0005-2795(79)90215-0
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
Publikováno v:
Archives of Biochemistry and Biophysics. 236:714-719
A quantitative yield of half-reduced (ferrous-ferric) cytochrome c peroxidase from Pseudomonas aeruginosa has been obtained by using either ascorbate or NADH as reductant of the resting (ferric-ferric) enzyme along with phenazine methosulfate as medi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bd379242dfe69d436660996b6f72d96
https://doi.org/10.1016/0003-9861(85)90677-0
https://doi.org/10.1016/0003-9861(85)90677-0
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
Autor:
Nils Ellfolk, Päivi Lehtovaara
Publikováno v:
European Journal of Biochemistry. 54:577-584
1 Leghemoglobin component a from Phaseolus vulgaris (kidney bean) was digested with trypsin; 15 tryptic peptides and free lysine were purified and the amino acid sequences of the peptides deter mined. 2 The internal order of the tryptic peptides was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ca9647789f208a257b7c28e446ffcf6
https://doi.org/10.1111/j.1432-1033.1975.tb04170.x
https://doi.org/10.1111/j.1432-1033.1975.tb04170.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