scholarly journals Rattlesnake cytochrome c. A re-appraisal of the reported amino acid sequence

1991 ◽  
Vol 274 (3) ◽  
pp. 825-831 ◽  
Author(s):  
R P Ambler ◽  
M Daniel
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Phylogenetic Trees ◽  
Attachment Site ◽  
British Library ◽  
Accelerated Evolution ◽  
C Terminus ◽  
Human Cytochrome ◽  
Human Cytochrome C

The amino acid sequence of rattlesnake cytochrome c was originally reported in 1965, and was one of the earlier sequences to be studied. When compared with other mitochondrial cytochromes c, the snake sequence was soon seen to be anomalous. There were several positions in which the snake protein resembled human cytochrome c, although comparable anomalies were not reported for the protein from other reptiles such as lizard and turtle. Explanations of these results have included accelerated evolution in the snake lineage, paralogy rather than orthology, and faulty determination of the sequence, and the rattlesnake is now often omitted from cytochrome c phylogenetic trees. We have re-investigated the sequence of the snake protein, and believe that the correct sequence differs in nine places from that used for evolutionary theorizing since 1965. Four of these differences are near the haem-attachment site, in a region that was only analysed for amino acid composition in the original investigation. The other five differences are towards the C-terminus of the molecule, and can be explained as being due to the wrong ordering of amino acids within peptides that had been satisfactorily purified. Despite these corrections, the rattlesnake cytochrome c sequence still more closely resembles human cytochrome c than it does that of any other protein we know. We believe that this is an example of convergent evolution, although it does appear that there has been accelerated change in the line connecting the rattlesnake to the ancestral vertebrate line. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50162 (16 pages) at the British Library Document Supply Centre, Boston Spa. Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1991) 273, 5.

scholarly journals The amino acid sequence of cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015

1973 ◽  
Vol 135 (4) ◽  
pp. 751-758 ◽  
Author(s):  
R. P. Ambler
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Attachment Site ◽  
Photosynthetic Bacterium ◽  
Chromatium Vinosum ◽  
British Library ◽  
Pseudomonas Denitrificans ◽  
Single Polypeptide Chain ◽  
C Terminus

The amino acid sequence of the cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015 (Iwasaki's ‘Pseudomonas denitrificans’) has been determined. This organism is the only non-photosynthetic bacterium in which the protein has been found. The protein consists of a single polypeptide chain of 127 residues, with a single haem covalently attached to two cysteines. Unlike normal cytochromes c, the haem attachment site is very close to the C-terminus. The amino acid sequence around the haem attachment site is very similar to that of Chromatium vinosum D cytochrome c′. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50022 at the British Library (Lending Division), (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

Amino Acid Replacement Studies of Human Cytochrome c by a Complementation System Using CYC1 Deficient Yeast

1988 ◽  
Vol 104 (3) ◽  
pp. 477-480 ◽  
Author(s):  
Yoshikazu Tanaka ◽  
Toshihiko Ashikari ◽  
Yuji Shibano ◽  
Teruo Amachi ◽  
Hajime Yoshizumi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Replacement ◽  
Human Cytochrome ◽  
Human Cytochrome C

scholarly journals The amino acid sequence of the cytochrome c-554(547) from the chemolithotrophic bacterium Thiobacillus neapolitanus

1985 ◽  
Vol 227 (3) ◽  
pp. 1009-1013 ◽  
Author(s):  
R P Ambler ◽  
T E Meyer ◽  
P A Trudinger ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Cysteine Residues ◽  
British Library ◽  
Thiobacillus Neapolitanus

An amino acid sequence is proposed for the cytochrome c-554(547) from the bacterium Thiobacillus neapolitanus N.C.I.B. 8539). It consists of a polypeptide chain of 91 residues, with a pair of haem-attachment cysteine residues at positions 15 and 18. There is similarity in sequence with each of the halves of the sequence of the dihaem cytochromes c4 and with a cytochrome c-554(548) from a halophilic strain of Paracoccus. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50127 (11 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1985) 225, 5.

scholarly journals Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation

2020 ◽  
Vol 21 (6) ◽  
pp. 2134
Author(s):  
Daniela Lalli ◽  
Camilla Rosa ◽  
Marco Allegrozzi ◽  
Paola Turano
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Axial Ligand ◽  
Heme Iron ◽  
Axial Coordination ◽  
Human Cytochrome ◽  
Alternative Amino Acid ◽  
Multiple Conformations ◽  
Human Cytochrome C ◽  
Distal Site

It is well known that axial coordination of heme iron in mitochondrial cytochrome c has redox-dependent stability. The Met80 heme iron axial ligand in the ferric form of the protein is relatively labile and can be easily replaced by alternative amino acid side chains under non-native conditions induced by alkaline pH, high temperature, or denaturing agents. Here, we showed a redox-dependent destabilization induced in human cytochrome c by substituting Phe82—conserved amino acid and a key actor in cytochrome c intermolecular interactions—with a Lys residue. Introducing a positive charge at position 82 did not significantly affect the structure of ferrous cytochrome c but caused localized unfolding of the distal site in the ferric state. As revealed by 1H NMR fingerprint, the ferric form of the F82K variant had axial coordination resembling the renowned alkaline species, where the detachment of the native Met80 ligand favored the formation of multiple conformations involving distal Lys residues binding to iron, but with more limited overall structural destabilization.

scholarly journals The amino acid sequence of cytochrome c from the locust, Schistocerca gregaria Forskal

1977 ◽  
Vol 163 (2) ◽  
pp. 333-338 ◽  
Author(s):  
A Lyddiatt ◽  
D Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Schistocerca Gregaria ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Cytochromes C ◽  
Single Polypeptide ◽  
Taxonomic Groups ◽  
Mitochondrial Cytochromes

The amino acid sequence of locust cytochrome c was determined, although the overlap between chymotryptic and tryptic peptides at residues tyrosine-97 and leucine-98 was not observed, owing to an anomalous tryptic break duplicating the chymotryptic digestion. The molecule consists of a single polypeptide chain of 107 residues, homologous with other mitochondrial cytochromes c. In common with other known insect cytochromes c, it possesses a non-acetylated, four-residue tail at the N-terminus relative to glycine-1 of the standard alignment. A molecular phylogeny for 17 species was constructed relating the cytochrome c molecules of Schistocerca gregaria and other invertebrates with those of representative taxonomic groups. Experimental details are given in a supplementary paper deposited as Supplementary Publication SUP 50077 (24 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can obtained on the terms indicated in Biochem. J. (1977) 161, 1.

scholarly journals The amino acid sequence of cytochrome c′ from the purple sulphur bacterium Chromatium vinosum

1979 ◽  
Vol 177 (3) ◽  
pp. 819-823 ◽  
Author(s):  
R P Ambler ◽  
M Daniel ◽  
T E Meyer ◽  
R G Bartsch ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Rhodospirillum Rubrum ◽  
Chromatium Vinosum ◽  
Peptide Sequence ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Purple Sulphur Bacterium

An amino acid sequence is proposed for the cytochrome c′ from the photosynthetic purple sulphur bacterium Chromatium vinosum strain D. It is single polypeptide chain of 131 residues, with haem-attachment cysteine residues at positions 121 and 124. The results discredit an earlier report [Dus, Bartsch & Kamen (1962) J. Biol. Chem 237, 3083–3093] of a di-haem peptide sequence from this protein. The sequence belongs to the same class as the published Alcal!igenes and Rhodospirillum rubrum cytochrome c′ squences, but the resemblance is not close. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50,093 (15 pp.) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1978) 169, 5.

scholarly journals Amino acid sequence of the Pronase-released heads of neuraminidase subtype N2 from the Asian strain A/Tokyo/3/67 of influenza virus

1982 ◽  
Vol 207 (1) ◽  
pp. 91-95 ◽  
Author(s):  
C W Ward ◽  
T C Elleman ◽  
A A Azad
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
British Library ◽  
Amino Acid Residues ◽  
Asian Strain ◽  
C Terminus ◽  
Glycosylation Sites ◽  
Neuraminidase Subtype

The amino acid sequence of the Pronase-released heads of neuraminidase subtype N2 from the A/Tokyo/3/67 strain of influenza virus was determined by a combination of peptide and nucleic acid sequence analysis. The results show that the Pronase-released heads contain 396 amino acid residues and extend from residue 74 in the original protein to the C-terminus at residue 469. The heads contain five potential glycosylation sites at asparagine residues 86, 146, 200, 234 and 402, but only the first four are glycosylated. The sequence homology with the corresponding region of the previously published sequence of the neuraminidase subtype N1 [Fields, Winter & Brownlee (1981) Nature (London) 290, 213-217] is 45%. Detailed evidence for the sequence data has been deposited as Supplementary Publication SUP 50116 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1981) 193, 5.

scholarly journals The amino acid sequence of cytochrome c-555 from the methane-oxidizing bacterium Methylococcus capsulatus

1986 ◽  
Vol 233 (2) ◽  
pp. 333-337 ◽  
Author(s):  
R P Ambler ◽  
H Dalton ◽  
T E Meyer ◽  
R G Bartsch ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Cysteine Residues ◽  
British Library ◽  
Methylococcus Capsulatus ◽  
Methionine Residue ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of the cytochrome c-555 from the obligate methanotroph Methylococcus capsulatus strain Bath (N.C.I.B. 11132) was determined. It is a single polypeptide chain of 96 residues, binding a haem group through the cysteine residues at positions 19 and 22, and the only methionine residue is a position 59. The sequence does not closely resemble that of any other cytochrome c that has yet been characterized. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50131 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment.

scholarly journals The purification and amino acid sequence of cytochrome c-552 from Euglena gracilis

1974 ◽  
Vol 139 (2) ◽  
pp. 449-459 ◽  
Author(s):  
G. W. Pettigrew
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Euglena Gracilis ◽  
Cytochrome F ◽  
Evolutionary Significance ◽  
British Library ◽  
Prosthetic Group ◽  
Amino Terminal ◽  
Lending Library

Cytochrome c-552 from Euglena gracilis was purified and the amino acid sequence determined. The protein is a single peptide chain of 87 residues with the haem prosthetic group bound through two thioether linkages to two cysteine residues near the amino-terminal region. The amino acid sequence shows some similarities to mitochondrial cytochrome c and to two prokaryote c-type cytochromes. The sequence, taken with the known characteristics of cytochrome c-552, indicates that it is an f-type cytochrome. The possible functional and evolutionary significance of these features in common is discussed. Detailed evidence for the amino acid sequence of Euglena cytochrome f has been deposited as Supplementary Publication SUP 50027 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7QB, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

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