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The amino acid sequences of the cytochromes c553 from Porphyridium cruentum and Aphanizomenon flos-aquae

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Abstract

The amino acid sequences of cytochrome c553 from the eukaryotic red alga Porphyridium cruentum and from the prokaryotic cyanobacterium Aphanizomenon flos-aquae have been determined from the tryptic and cyanogen bromide peptides. The results indicate that a charged region of these proteins has evolved with special rapidity to accomodate a rapid evolution of a binding site in the P700 electron acceptor complex.

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Authors and Affiliations

  1. Department of Biochemistry, Purdue University, 47907, West Lafayette, IN, USA

    James R. Sprinkle, Mark Hermodson & David W. Krogmann

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  1. James R. Sprinkle
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  2. Mark Hermodson
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  3. David W. Krogmann
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Sprinkle, J.R., Hermodson, M. & Krogmann, D.W. The amino acid sequences of the cytochromes c553 from Porphyridium cruentum and Aphanizomenon flos-aquae . Photosynth Res 10, 63–73 (1986). https://doi.org/10.1007/BF00024186

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  • DOI: https://doi.org/10.1007/BF00024186

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