THE AMINO ACID SEQUENCE OF CYTOCHROMEcIN RELATION TO ITS FUNCTION AND EVOLUTION

1964 ◽  
Vol 42 (6) ◽  
pp. 745-753 ◽  
Author(s):  
E. Margoliash
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
The Other ◽  
Functional Activities ◽  
Cytochromes C ◽  
The One ◽  
Structural Aspects

A comparison of the amino acid sequences of the cytochromes c from horse, pig, rabbit, chicken, and man leads to the conclusion that all have derived phylogenetically from a common primordial cytochrome c. The significance of the constant and of the variable features of these sequences with regard, on the one hand, to the structural aspects of the functional activities of the protein, and on the other, to the evolutionary relations between the various cytochromes c is discussed.

scholarly journals The amino acid sequence of cytochromes c-551 from three species of Pseudomonas

1973 ◽  
Vol 131 (3) ◽  
pp. 485-498 ◽  
Author(s):  
R. P. Ambler ◽  
Margaret Wynn
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Mitochondrial Cytochrome ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Peptide

The amino acid sequences of the cytochromes c-551 from three species of Pseudomonas have been determined. Each resembles the protein from Pseudomonas strain P6009 (now known to be Pseudomonas aeruginosa, not Pseudomonas fluorescens) in containing 82 amino acids in a single peptide chain, with a haem group covalently attached to cysteine residues 12 and 15. In all four sequences 43 residues are identical. Although by bacteriological criteria the organisms are closely related, the differences between pairs of sequences range from 22% to 39%. These values should be compared with the differences in the sequence of mitochondrial cytochrome c between mammals and amphibians (about 18%) or between mammals and insects (about 33%). Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50015 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.

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 Nigella damascena L. (love-in-a-mist)

1973 ◽  
Vol 133 (2) ◽  
pp. 251-254 ◽  
Author(s):  
R. H. Brown ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
The Other ◽  
Carboxypeptidase A ◽  
Cytochromes C ◽  
Lending Library ◽  
Nigella Damascena

The amino acid sequence of cytochrome c from Nigella damascena L. was determined on 0.2μmol of protein. Peptides from a single chymotryptic digest were analysed by the dansyl–Edman procedure. These peptides were ordered by reference to the sequences of other plant cytochromes c, assuming that the Nigella cytochrome is homologous with the other cytochromes. Many of the Nigella peptides were one or two residues short when compared with the corresponding chymotryptic peptides from other plant cytochromes c. These residues are assumed to have been removed by an endogenous carboxypeptidase, and the identification and placing of these residues is entirely based on homology. These residues are numbered 3, 18, 42, 43, 44, 54, 67, 72, 73, 82 and 105. A number of other positions are almost entirely placed by homology. These are positions which could not be placed definitely by dansyl–Edman analysis or by dansylation after digestion with carboxypeptidase A, and are numbered 14, 15, 16, 39, 40, 85, 86, 87 and 88. Except for residue 15, all residues based entirely, or nearly so, on homology have been previously found invariant in sequences of plant cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50017, 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.

scholarly journals The amino acid sequence of cytochrome c from Abutilon theophrasti Medic. and Gossypium barbadense L. (cotton)

1971 ◽  
Vol 124 (4) ◽  
pp. 787-791 ◽  
Author(s):  
E. W. Thompson ◽  
B. A. Notton ◽  
M. Richardson ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
Gossypium Barbadense ◽  
Abutilon Theophrasti ◽  
Amino Acid Sequences ◽  
Cytochromes C ◽  
Lending Library

The amino acid sequences of Abutilon and Gossypium cytochromes c were determined on 1μmol of protein. The molecules consist of 111 residues and are homologous with other mitochondrial plant 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 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 Structural role of the tyrosine residues of cytochrome c

1982 ◽  
Vol 205 (1) ◽  
pp. 153-165 ◽  
Author(s):  
C G Eley ◽  
G R Moore ◽  
R J Williams ◽  
W Neupert ◽  
P J Boon ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Resolution ◽  
Cytochrome C ◽  
Amino Acid Sequences ◽  
The Other ◽  
Amino Acid Substitutions ◽  
Tertiary Structures ◽  
Tyrosine Residues ◽  
Cytochromes C

The tertiary structures of horse, tuna, Neurospora crassa, horse [Hse65,Leu67]- and horse [Hse65,Leu74]-cytochromes c were studied with high-resolution 1H n.m.r. spectroscopy. The amino acid sequences of these proteins differ at position 46, which is occupied by phenylalanine in the horse proteins but by tyrosine in the remaining two, and at positions 67, 74 and 97, which are all occupied by tyrosine residues in horse and tuna cytochrome c but in the other proteins are substituted by phenylalanine or leucine, though there is only one such substitution per protein. The various aromatic-amino-acid substitutions do not seriously affect the protein structure.

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.

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1969 ◽  
Vol 24 (7) ◽  
pp. 877-885 ◽  
Author(s):  
H. G. Wittmann ◽  
I. Hindennach ◽  
B. Wittmann-Liebold
Keyword(s):  
Experimental Data ◽  
Amino Acids ◽  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Spatial Structure ◽  
Amino Acid Sequences ◽  
The Other ◽  
Tryptic Peptides ◽  
Tmv Strains

Experimental data for determining a) the amino acid sequences of eight tryptic peptides containing 95 amino acids and b) the order of the tryptic peptides are given. Combining the data of this and of a previous paper the complete amino acid sequence of the coat protein of the TMV strain Holmes rib grass (HRG) is established (Fig. 5). It is compared with three other TMV strains the sequences of which have been determined before (Fig. 6).Differences and similarities between the sequences of the four TMV strains are discussed. HRG has a deletion of two amino acids and it is the most distantly related of the four TMV strains. When the sequence of HRG is compared to that of any of the other strains it turns out that in each case more than 50% of the 156 positions contain different amino acids (Fig. 7).The number of positions with the same amino acid in all strains and mutants so far studied is 30 per cent. These positions are not randomly distributed but clustered mainly in two regions. This finding probably reflects the restriction of amino acid exchanges by the spatial structure of the viral rod.

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 Allium porrum L. (leek)

1973 ◽  
Vol 131 (2) ◽  
pp. 247-251 ◽  
Author(s):  
R. H. Brown ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Science And Technology ◽  
Allium Porrum ◽  
Cytochromes C ◽  
Lending Library ◽  
Mitochondrial Origin

The amino acid sequence of leek cytochrome c was determined with 0.4μmol of protein. The sequence was deduced solely from a chymotryptic digest. The cytochrome was homologous with other plant cytochromes c of mitochondrial origin. Leek cytochrome c has an N-acetylated ‘tail’ as compared with mammalian cytochrome c, and two residues of ε-N-trimethyl-lysine. Unlike other plant cytochromes c, leek cytochrome c has glutamic acid or glutamine in position 11, leucine in position 20 and alanine in position 51. 4-Hydroxyproline partially substitutes for proline in position 79. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50012, 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.

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