Mitochondrial cytochrome b: evolution and structure of the protein

Degli Esposti, Mauro; De Vries, Simon; Crimi, Massimo; Ghelli, Anna; Patarnello, Tomaso; Meyer, Axel

Mitochondrial cytochrome b: evolution and structure of the protein

Dateien

Mitochondrial_cytochrome_b_evolution_and_structure_1993.pdfGröße: 6.77 MBDownloads: 3950

Datum

1993

Autor:innen

Degli Esposti, Mauro

De Vries, Simon

Crimi, Massimo

Ghelli, Anna

Patarnello, Tomaso

Meyer, Axel

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biochimica et Biophysica Acta. 1993, 1143(3), pp. 243-271. ISSN 0005-2728. Available under: doi: 10.1016/0005-2728(93)90197-N

Zusammenfassung

Cytochrome b is the central redox catalytic subunit of the quinol cytochrome c or plastocyanin oxidoreductases. It is involved in the binding of the quinone
substrate and it is responsible for the transmembrane electron transfer by which redox energy is converted into a protonmotive force Cytochrome b also contains the sites to which various inhibitors and quinone antagonists bind and, consequently, inhibit the oxidoreductase. Ten partial primary sequences of cytochrome b are presented here and they are compared with sequence data from over 800 species for a detailed analysis of the natural variation in the protein. This sequence information has been used to predict some aspects of the structure of the protein, in particular the folding of the transmembrane helices and the location of the quinone- and heme-binding pockets. We have observed that inhibitor sensitivity vanes greatly among species. The comparison of inhibition titrations in combination with the analysis of the primary structures has enabled us to identify amino acid residues in cytochrome b that may be mvolved m the binding of the inhibitors and, by extrapolation, quinone/quinol. The information on the quinone-binding sites obtained in this way is expected to be both complementary and supplementary to that which will be obtained in the future by mutagenesis and X-ray crystallography.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

Cytochrome b, Ubiquinone, Respiration mhibition, Amino acid sequence, Mitochondrial DNA sequence, DNA, Molecular evolution

Zitieren

ISO 690

DEGLI ESPOSTI, Mauro, Simon DE VRIES, Massimo CRIMI, Anna GHELLI, Tomaso PATARNELLO, Axel MEYER, 1993. Mitochondrial cytochrome b: evolution and structure of the protein. In: Biochimica et Biophysica Acta. 1993, 1143(3), pp. 243-271. ISSN 0005-2728. Available under: doi: 10.1016/0005-2728(93)90197-N

BibTex

@article{DegliEsposti1993Mitoc-7455,
  year={1993},
  doi={10.1016/0005-2728(93)90197-N},
  title={Mitochondrial cytochrome b: evolution and structure of the protein},
  number={3},
  volume={1143},
  issn={0005-2728},
  journal={Biochimica et Biophysica Acta},
  pages={243--271},
  author={Degli Esposti, Mauro and De Vries, Simon and Crimi, Massimo and Ghelli, Anna and Patarnello, Tomaso and Meyer, Axel}
}

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