scholarly journals The cellular location and specificity of bacterial cytochrome c peroxidases

1990 ◽  
Vol 271 (3) ◽  
pp. 707-712 ◽  
Author(s):  
C F Goodhew ◽  
I B Wilson ◽  
D J Hunter ◽  
G W Pettigrew
Keyword(s):  
Cytochrome C ◽  
Paracoccus Denitrificans ◽  
Pseudomonas Stutzeri ◽  
Cytochrome C Peroxidase ◽  
Total Activity ◽  
Gram Negative Bacteria ◽  
Visible Absorption ◽  
Cellular Compartment ◽  
Cytochromes C ◽  
Mitochondrial Cytochromes

The locations of cytochrome c peroxidase and catalase activities in the two Gram-negative bacteria Pseudomonas stutzeri (N.C.I.B. 9721) and Paracoccus denitrificans (N.C.I.B. 8944) were investigated by the production of spheroplasts. In both species the cytochrome c peroxidase was predominantly periplasmic: 92% of total activity in Ps. stutzeri and 98% of nonmembrane-bound activity in Pa. denitrificans were found in this cellular compartment. In contrast, the catalase was mostly in the cytoplasmic fraction. Purification of the Pa. denitrificans cytochrome c peroxidase showed it to be the haem c-containing polypeptide of Mr 42,000 that has already been described by Bosma, Braster, Stouthamer & Van Versefeld [(1987) Eur. J. Biochem. 165, 665-670] but was not identified by them as a peroxidase. The visible-absorption spectra of the enzyme closely resemble those of cytochrome c peroxidase from Pseudomonas aeruginosa but the donor specificity is different, with the Pa. denitrificans enzyme preferring the basic mitochondrial cytochromes c to the acidic cytochromes c-551 and reacting well with the Pa. denitrificans cytochrome c-550.

scholarly journals Physicochemical properties of two atypical cytochromes c, Crithidia cytochrome c-557 and Euglena cytochrome c-558

1975 ◽  
Vol 149 (1) ◽  
pp. 155-167 ◽  
Author(s):  
G W Pettigrew ◽  
I Aviram ◽  
A Schejter
Keyword(s):  
Cytochrome C ◽  
Physicochemical Properties ◽  
High Spin ◽  
Visible Spectrum ◽  
Prosthetic Group ◽  
Ph Values ◽  
Cytochromes C ◽  
Kinetics Of ◽  
Alkaline Isomerization ◽  
Mitochondrial Cytochromes

Cytochrome c-557 from Crithidia oncopelti and cytochrome c-558 from Euglena gracilis are mitochondrial cytochromes c that have an atypical haem-binding site. It was of interest to know whether the loss of one thioether bond affected the physicochemical properties of these cytochromes. The thermodynamic parameters of the redox potential were measured. The reaction with imidazole, the kinetics and thermodynamics of the alkaline isomerization and the effect of heating on the visible spectrum are described for the ferricytochromes. The kinetics of the loss of cyanide, the spectral changes occurring on reduction with dithionite at alkaline pH values and the reactivity with CO are described for the ferrocytochromes. In many respects the cytochromes of the two protozoans are very similar to the cytochromes of horse and yeast. The ferricytochromes do, however, undergo a reversible transition to high-spin species on heating, which may be due to the more flexible attachment of the prosthetic group. Similarly the alkaline isomers of cytochromes c-557 and c-558 give rise to high-spin proteins above pH 11. The alkaline isomerization of cytochrome c-558, involves a pKobs. of 10 and kinetics which do not obey the model of Davis et al. [(1974) J. Biol. Chem.249, 2624-2632] for horse cytochrome c. It is proposed that a model involving two ionizations, followed by a conformation change, may fit the data. Both cytochromes c-557 and c-558 combine slowly with CO at neutral pH values.

scholarly journals The amino acid sequence of cytochrome c of Fagopyrum esculentum Moench (buckwheat) and Brassica oleracea L. (cauliflower)

1971 ◽  
Vol 124 (4) ◽  
pp. 783-785 ◽  
Author(s):  
E. W. Thompson ◽  
M. Richardson ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Brassica Oleracea ◽  
Amino Acid Sequences ◽  
Cytochromes C ◽  
Lending Library ◽  
Fagopyrum Esculentum Moench ◽  
Mitochondrial Cytochromes ◽  
Brassica Oleracea L

The amino acid sequences of buckwheat and cauliflower cytochromes c were determined on 1½μmol and 1μmol of protein respectively. The molecules consist of 111 residues and are homologous with other plant mitochondrial cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50005 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1971), 121, 7.

scholarly journals Separate binding sites for antimycin and mucidin in the respiratory chain of the bacterium Paracoccus denitrificans and their occurrence in other denitrificans bacteria

1988 ◽  
Vol 252 (3) ◽  
pp. 905-908 ◽  
Author(s):  
I Kucera ◽  
R Hedbávný ◽  
V Dadák
Keyword(s):  
Respiratory Chain ◽  
Binding Sites ◽  
Paracoccus Denitrificans ◽  
Pseudomonas Stutzeri ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Q Cycle ◽  
Cytochromes C ◽  
Fluorimetric Titration

By means of the method of fluorimetric titration it has been shown that mucidin does not affect the attachment of antimycin to membranes from anaerobically grown Paracoccus denitrificans. The fluorimetric titration with antimycin can be used in the determination of the amount of the cytochrome bc1 complex in the membrane. In cells inhibited with antimycin, the oxidation of cytochromes c was accompanied by the reduction of cytochrome b; in the presence of mucidin this effect did not take place. The results, which indicated a difference in binding sites, were interpreted in terms of the Q-cycle [Mitchell (1976) J. Theor. Biol. 62, 327-367; Trumpower (1981) Biochim. Biophys. Acta 639, 129-155]. Comparable sensitivity towards antimycin and mucidin was shown by other typical denitrifying bacteria: Pseudomonas stutzeri and Alcaligenes xylosoidans, subspecies denitrificans.

scholarly journals The amino acid sequence of cytochrome c from Spinacea oleracea L. (spinach)

1973 ◽  
Vol 131 (2) ◽  
pp. 253-256 ◽  
Author(s):  
R. H. Brown ◽  
M. Richardson ◽  
R. Scogin ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
Spinacea Oleracea ◽  
Cytochromes C ◽  
Lending Library ◽  
Mitochondrial Cytochromes

The amino acid sequence of spinach (Spinacea oleracea L., var. Monster Viroflay) cytochrome c was determined on 1μmol of protein. The molecule consists of 111 residues and is homologous with other mitochondrial cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50013, at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

The mechanism of activation of cytochrome c peroxidase from Paracoccus denitrificans

1997 ◽  
Vol 67 (1-4) ◽  
pp. 88
Author(s):  
Isabel Moura ◽  
S. Prazeres ◽  
C. Moreno ◽  
H. Lopes ◽  
G. Pettigrew ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Paracoccus Denitrificans ◽  
Cytochrome C Peroxidase

Ca2+ and the bacterial peroxidases: the cytochrome c peroxidase from Pseudomonas stutzeri

2003 ◽  
Vol 8 (1) ◽  
pp. 29-37 ◽  
Author(s):  
Cristina G. Timóteo ◽  
Pedro Tavares ◽  
Celia F. Goodhew ◽  
Luís C. Duarte ◽  
Kornelia Jumel ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Pseudomonas Stutzeri ◽  
Cytochrome C Peroxidase

Analysis of the activation mechanism of Pseudomonas stutzeri cytochrome c peroxidase through an electron transfer chain

2011 ◽  
Vol 16 (6) ◽  
pp. 881-888 ◽  
Author(s):  
P. M. Paes de Sousa ◽  
D. Rodrigues ◽  
C. G. Timóteo ◽  
M. L. Simões Gonçalves ◽  
G. W. Pettigrew ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Pseudomonas Stutzeri ◽  
Cytochrome C Peroxidase ◽  
Activation Mechanism ◽  
Electron Transfer Chain ◽  
Transfer Chain
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