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Structural Studies of Euglena Cytochrome C 1

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Bioenergetics

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Summary

Euglena gracilis complex III prepared from its submitochondrial particles showed an atypical difference absorption spectrum for cytochrome c1 with α-peak at 561 nm. Pyridine ferrohemochrome of cytochrome c1 showed its α-peak at 553 nm. The amino-terminal sequence of cytochrome c1 suggested that its heme moiety was covalently linked to cysteine-39 through a single thioether bond. Phenylalanine occupied position 36 usually occupied by cysteine affording the other thioether bond. The total amino acid sequence of mature cytochrome c1 was determined by sequencing of its cDNA. The cDNA clone consisted of 872 base pairs encoding the mature protein with 243 amino acids. The putative sequence contained an unusual heme binding sequence, -F-A-P-C-H-, instead of the typical sequence, -C-X-Y-C-H-, found in other eukaryotic C-type cytochromes. Sequence comparison, gene manipulation, and physical studies indicated the heme ligands and a binding site to cytochrome c.

This work was supported in part by Grants-in-Aid for Scientific Research on Priority Area of Bioenergetics and on Nos. 01470148 and 62470148 from the Ministry of Education, Science and Culture of Japan.

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Author notes

  1. Kuniaki Mukai

    Present address: Mitsubishi-Kasei Institute of Life Science, Machida, Tokyo 194, Japan

Authors and Affiliations

  1. Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan

    Hiroshi Matsubara, Kuniaki Mukai & Sadao Wakabayashi

Authors
  1. Hiroshi Matsubara
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  2. Kuniaki Mukai
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  3. Sadao Wakabayashi
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Editor information

Editors and Affiliations

  1. Rensselaer Polytechnic Institute, Troy, New York, USA

    Chong H. Kim

  2. University of Nagoya, Nogoya, Japan

    Takayuki Ozawa

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© 1990 Plenum Press, New York

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Matsubara, H., Mukai, K., Wakabayashi, S. (1990). Structural Studies of Euglena Cytochrome C 1 . In: Kim, C.H., Ozawa, T. (eds) Bioenergetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5835-0_11

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  • DOI: https://doi.org/10.1007/978-1-4684-5835-0_11

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5837-4

  • Online ISBN: 978-1-4684-5835-0

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