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 Short Communications. A comparative study of some kinetic and spectral properties of guanidinated and native cytochrome c

1975 ◽  
Vol 147 (1) ◽  
pp. 175-177 ◽  
Author(s):  
T Brittain ◽  
C Greenwood
Keyword(s):  
Cytochrome C ◽  
Comparative Study ◽  
Spectral Properties ◽  
Visible Spectrum ◽  
Kinetic Properties ◽  
Chemically Modified ◽  
Effects Of Ph ◽  
Kinetics Of ◽  
Kinetics Of Reduction

An investigation of the spectral and some kinetic properties of a chemically modified cytochrome c is presented. The kinetics of reduction by chromous ion and ascorbate are shown to be unchanged from that of the native molecule, as are the kinetics of NO binding. The effects of pH on the visible spectrum are discussed in terms of a possible change in the pattern of co-ordination of the molecule with changing pH.

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 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.

Thermodynamics and kinetics of reduction and species conversion at a hydrophobic surface for mitochondrial cytochromes c and their cardiolipin adducts

2015 ◽  
Vol 176 ◽  
pp. 1019-1028 ◽  
Author(s):  
Antonio Ranieri ◽  
Giulia Di Rocco ◽  
Diego Millo ◽  
Gianantonio Battistuzzi ◽  
Carlo A. Bortolotti ◽  
...  
Keyword(s):  
Hydrophobic Surface ◽  
Thermodynamics And Kinetics ◽  
Cytochromes C ◽  
Kinetics Of ◽  
Kinetics Of Reduction ◽  
Mitochondrial Cytochromes

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 The amino acid sequence of cytochrome c from Cucurbita maxima L. (pumpkin)

1971 ◽  
Vol 124 (4) ◽  
pp. 779-781 ◽  
Author(s):  
E. W. Thompson ◽  
M. Richardson ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
Cucurbita Maxima ◽  
Cytochromes C ◽  
Lending Library ◽  
Mitochondrial Cytochromes

The amino acid sequence of pumpkin cytochrome c was determined on 2μmol of protein. Some evidence was found for the occurrence of two forms of cytochrome c, whose sequences differed in three positions. Pumpkin cytochrome c consists of 111 residues and is homologous with mitochondrial cytochromes c from other plants. 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 The amino acid sequence of cytochrome c from Helix aspersa Müller (garden snail)

1972 ◽  
Vol 128 (4) ◽  
pp. 971-974 ◽  
Author(s):  
R. H. Brown ◽  
M. Richardson ◽  
D. Boulter ◽  
J. A. M. Ramshaw ◽  
R. P. S. Jefferies
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Blocking Group ◽  
Single Polypeptide Chain ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Polypeptide ◽  
Mitochondrial Cytochromes

The amino acid sequence of a snail cytochrome c has been determined. The molecule consists of a single polypeptide chain of 104 residues, and is homologous with other mitochondrial cytochromes c. Unlike the cytochromes c from vertebrates, there is no acetyl blocking group at the N-terminus. A change in an otherwise invariant position has been observed in position 87. Comparison with amino acid sequences of cytochromes c from other sources indicates that the point of divergence of the molluscs and the vertebrates in evolutionary time was 720 million years ago. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50009 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. (1972), 126, 5.

scholarly journals Amino acid sequence of cytochrome c from Tetrahymena pyriformis Phenoset A

1976 ◽  
Vol 159 (2) ◽  
pp. 193-199 ◽  
Author(s):  
G E Tarr ◽  
W M Fitch
Keyword(s):  
Cytochrome C ◽  
Sequence Data ◽  
Tetrahymena Pyriformis ◽  
Complete Sequence ◽  
Terminal Region ◽  
British Library ◽  
Homologous Proteins ◽  
Cytochromes C ◽  
Relationship Of ◽  
Mitochondrial Cytochromes

The cytochrome c of Tetrahymena pyriformis GL (Phenoset A) had an isoelectric point of 6.5 and by sequence the following composition: Asp(7) Asn(2) Thr(4) Ser(8) Glu(6) Gln(2) Pro(7) Gly(13) Ala(13) Val(7) Met(2) Ile(5) Leu(6) Tyr(2) Phe(5) Lys(11) His(3) Trp(1) Arg(3) Cys(2) (total 109 residues). The peptides derived from the protein afforded complete overlap, so a complete sequence could be determined without reference of homologous proteins. Alignment with other mitochondrial cytochromes c required two internal deletions totalling three residues and an N-terminal region two residues longer than, and a C-terminal region one residue shorter than, the previously known limits. The sequence was the most divergent of the known mitochondrial cytochromes c, suggesting a distant relationship of ciliates to other eukaryotes. Details of the sequence data have been deposited as Supplementary Publication no. SUP 50068 (37 pages) at The British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7 BQ, U.K., from whom copies can be obtained on the terms given in Biochem. J. (1976) 153,5.

scholarly journals The kinetics of the oxidation of cytochrome c by Paracoccus cytochrome c peroxidase

1994 ◽  
Vol 300 (3) ◽  
pp. 907-914 ◽  
Author(s):  
R Gilmour ◽  
C F Goodhew ◽  
G W Pettigrew ◽  
S Prazeres ◽  
J J Moura ◽  
...  
Keyword(s):  
Cytochrome C ◽  
High Spin ◽  
Spin State ◽  
Paracoccus Denitrificans ◽  
Cytochrome C Peroxidase ◽  
High Spin State ◽  
Enzyme Activation ◽  
First Order ◽  
Ferrocytochrome C ◽  
Kinetics Of

In work that is complementary to our investigation of the spectroscopic features of the cytochrome c peroxidase from Paracoccus denitrificans [Gilmour, Goodhew, Pettigrew, Prazeres, Moura and Moura (1993) Biochem. J. 294, 745-752], we have studied the kinetics of oxidation of cytochrome c by this enzyme. The enzyme, as isolated, is in the fully oxidized form and is relatively inactive. Reduction of the high-potential haem at pH 6 with ascorbate results in partial activation of the enzyme. Full activation is achieved by addition of 1 mM CaCl2. Enzyme activation is associated with formation of a high-spin state at the oxidized low-potential haem. EGTA treatment of the oxidized enzyme prevents activation after reduction with ascorbate, while treatment with EGTA of the reduced, partially activated, form abolishes the activity. We conclude that the active enzyme is a mixed-valence form with the low-potential haem in a high-spin state that is stabilized by Ca2+. Dilution of the enzyme results in a progressive loss of activity, the extent of which depends on the degree of dilution. Most of the activity lost upon dilution can be recovered after reconcentration. The M(r) of the enzyme on molecular-exclusion chromatography is concentration-dependent, with a shift to lower values at lower concentrations. Values of M(r) obtained are intermediate between those of a monomer (39,565) and a dimer. We propose that the active form of the enzyme is a dimer which dissociates at high dilution to give inactive monomers. From the activity of the enzyme at different dilutions, a KD of 0.8 microM can be calculated for the monomerdimer equilibrium. The cytochrome c peroxidase oxidizes horse ferrocytochrome c with first-order kinetics, even at high ferrocytochrome c concentrations. The maximal catalytic-centre activity (‘turnover number’) under the assay conditions used is 62,000 min-1, with a half-saturating ferrocytochrome c concentration of 3.3 microM. The corresponding values for the Paracoccus cytochrome c-550 (presumed to be the physiological substrate) are 85,000 min-1 and 13 microM. However, in this case, the kinetics deviate from first-order progress curves at all ferrocytochrome c concentrations. Consideration of the periplasmic environment in Paracoccus denitrificans leads us to propose that the enzyme will be present as the fully active dimer supplied with saturating ferrocytochrome c-550.

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