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. 1989 Nov 1;263(3):981–984. doi: 10.1042/bj2630981

The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus.

S Wakabayashi 1, T Kimura 1, K Fukuyama 1, H Matsubara 1, L J Rogers 1
PMCID: PMC1133529  PMID: 2597140

Abstract

The amino acid sequence of the constitutive flavodoxin from the red alga Chondrus crispus was determined from the analyses of peptide fragments derived by enzymic digestions of the carboxymethylated protein. This is the first sequence reported for a flavodoxin from a eukaryote. The protein is composed of 173 amino acid residues and is a member of the longer-chain group of flavodoxins. The extent of sequence homology to the three other flavodoxins in the group for which sequences are available is in the range 36-39%, with the most strongly conserved regions being those implicated in binding of the FMN, the redox-active prosthetic group. Nevertheless, Chondrus crispus flavodoxin stands apart in a number of respects, in particular the possession of an unusually high content of proline, with these residues distributed more or less regularly along the peptide chain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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