The Journal of General and Applied Microbiology
Online ISSN : 1349-8037
Print ISSN : 0022-1260
ISSN-L : 0022-1260
THE PRIMARY STRUCTURE OF CLOSTRIDIUM PERFRINGENS FERREDOXIN
YASUHIDE SEKISACHIKO SEKIMAKOTO ISHIMOTO
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1989 Volume 35 Issue 3 Pages 167-172

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Abstract

The complete amino acid sequence of ferredoxin from Clostridium perfringens was established by a combination of Edman degradation and protease digestion. The sequence was: AYKILDTCVSCGACAAECPV-DAISQGDTQFVIDADTCIDCGNCANVCPVGAPVQE. It shows a high degree of similarity to Clostridium pasteurianum ferredoxin (89% homology), and its residual conversions are located at the non-conservative sites of the clostridial-type ferredoxins: at 6 sites, discrete except for the last two, all along the amino(N)-terminal half of the chain, while none at the carboxyl(C)-terminal half (residue numbers from 30 to 55). The occurrence of the 8 cysteine residues at the conservative sites strongly suggested the presence of the conventional two [4Fe-4S] clusters in the molecule.

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