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Ferredoxin isoforms from Chlorella vulgaris (Chlorococcales, Chlorophyceae): Molecular characterization and participation in ferredoxin‐dependent enzymes
Author(s) -
Kanno Toshihiro,
Nakayama Hidenori,
Shinpo Kunihiro,
Masada Masahiro,
Tamura Goro
Publication year - 1995
Publication title -
phycological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.438
H-Index - 44
eISSN - 1440-1835
pISSN - 1322-0829
DOI - 10.1111/j.1440-1835.1995.tb00021.x
Subject(s) - ferredoxin , biology , isoelectric point , chlorophyceae , spinach , chlorella vulgaris , ferredoxin—nadp(+) reductase , isoelectric focusing , enzyme , botany , biochemistry , algae , chlorophyta
SUMMARY Using hydrophobic chromatography, Chlorella ferredoxin was separated into three components (Fd I, Fd II and Fd III) in ratios of approximately 3:13:1. The three components differed in isoelectric point, peptide mapping, amino acid composition and N‐terminal sequence. Fd II and Fd III were found to support fairly high rates of cytochrome c reduction by spinach FNR, while Fd I could not support this reaction at all. The highest value of the specificity constant (k cat /K m for NiR was demonstrated for Fd II‐dependent activity; however, the lowest value of k cat /K m for NiR was obtained using Fd II.