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Home / Equine Research Bank / Proc Natl Acad Sci U S A / Primary structure determination of two cytochromes c2: close...
Proceedings of the National Academy of Sciences of the United States of America1976; 73(2); 472-475; doi: 10.1073/pnas.73.2.472

Primary structure determination of two cytochromes c2: close similarity to functionally unrelated mitochondrial cytochrome C.

Abstract: The amino-acid sequences of the cytochromes c2 from the photosynthetic non-sulfur purple bacteria Rhodomicrobium vannielii and Rhodopseudomonas viridis have been determined. Only a single residue deletion (at position 11 in horse cytochrome c) is necessary to align the sequences with those of mitochondrial cytochromes c. The overall sequence similarity between these cytochromes c2 and mitochondrial cytochromes c is closer than that between mitochondrial cytochromes c and the other cytochromes c2 of known sequence, and in the latter multiple insertions and deletions must be postulated before a match can be obtained. Nevertheless, these two cytochromes c2 show no better reactivity with the mitochondrial cytochrome c oxidase than do the less well-matched cytochromes c2. The bearing of these findings on possible evolutionary relationship between mitochondria and prokaryotes is discussed.
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Publication Date: 1976-02-01 PubMed ID: 174109PubMed Central: PMC335931DOI: 10.1073/pnas.73.2.472Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article delves into the study of amino-acid sequences of the cytochromes c2 from two types of photosynthetic non-sulfur purple bacteria. The findings show a close similarity with mitochondrial cytochrome c and discuss the possible evolutionary relationship between mitochondria and prokaryotes.

Amino-acid sequences of Cytochromes c2

  • The study involved the determination of the amino-acid sequences of cytochromes c2 from two types of photosynthetic non-sulfur purple bacteria – Rhodomicrobium vannielii and Rhodopseudomonas viridis.
  • Researchers have highlighted that when the sequences are aligned with those of mitochondrial cytochromes c, only a single residue deletion is needed at position 11 of horse cytochrome c.

Sequence Similarity

  • The overall sequence similarity between these cytochromes c2 and mitochondrial cytochromes c is closer than between mitochondrial cytochromes c and the other cytochromes c2 that have known sequences.
  • However, the alignment of the other cytochromes c2 sequences with mitochondrial cytochromes c requires multiple insertions and deletions before a match can be obtained.

Reactivity with Mitochondrial Cytochrome c Oxidase

  • The two cytochromes c2, despite their closer sequence similarity, do not show better reactivity with the mitochondrial cytochrome c oxidase than the less well-matched cytochromes c2.
  • This implies that the sequence similarity does not directly influence the reactivity level with mitochondrial cytochrome c oxidase.

Possible Evolutionary Relationship

  • The study discusses the implications of these findings on the possible evolutionary relationship between mitochondria and prokaryotes.
  • Despite the similar amino-acid sequence, the difference in reactivity levels with the mitochondrial cytochrome c oxidase indicates that function and sequence similarity may not always correlate.

Cite This Article

APA
Ambler RP, Meyer TE, Kamen MD. (1976). Primary structure determination of two cytochromes c2: close similarity to functionally unrelated mitochondrial cytochrome C. Proc Natl Acad Sci U S A, 73(2), 472-475. https://doi.org/10.1073/pnas.73.2.472

Publication

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
NlmUniqueID: 7505876
Country: United States
Language: English
Volume: 73
Issue: 2
Pages: 472-475

Researcher Affiliations

Ambler, R P
    Meyer, T E
      Kamen, M D

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Cytochrome c Group
        • Cytochromes
        • Horses
        • Mitochondria / enzymology
        • Rhodopseudomonas / enzymology
        • Rhodospirillaceae / enzymology
        • Species Specificity

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        Citations

        This article has been cited 12 times.
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        2. Wodara C, Bardischewsky F, Friedrich CG. Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB17: essential role of sulfite dehydrogenase in lithotrophic sulfur oxidation.. J Bacteriol 1997 Aug;179(16):5014-23.
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          doi: 10.1007/BF00933729pubmed: 6087241google scholar: lookup
        5. Ambler RP, Dalton H, Meyer TE, Bartsch RG, Kamen MD. The amino acid sequence of cytochrome c-555 from the methane-oxidizing bacterium Methylococcus capsulatus.. Biochem J 1986 Jan 15;233(2):333-7.
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        6. Ambler RP, Meyer TE, Cusanovich MA, Kamen MD. The amino acid sequence of the cytochrome c2 from the phototrophic bacterium Rhodopseudomonas globiformis.. Biochem J 1987 Aug 15;246(1):115-20.
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