Chlorella vulgaris aldehyde reductase is capable of functioning as ferric reductase and of driving the fenton reaction in the presence of free flavin.
The free flavin-dependent Fenton reaction was detected in cell-free extracts of Chlorella. The corresponding enzyme was purified to homogeneity, and its N-terminal sequence was highly homologous to those of aldo-keto reductase family enzymes. The purified enzyme displayed aldehyde reductase activity in the presence of NADPH. Additionally, it showed ferric reductase activity and drove the Fenton reaction in the presence of free FAD and NADH.
Sato
Junichi
J
Department of Bioscience, Tokyo University of Agriculture, Japan.
Takeda
Kouji
K
Nishiyama
Rika
R
Fusayama
Kouichi
K
Arai
Toshiaki
T
Sato
Takumi
T
Watanabe
Toshihiro
T
Abe
Akira
A
Nakagawa
Junichi
J
Kawasaki
Shinji
S
Niimura
Youichi
Y
D000429:Alcohol Oxidoreductases; D000449:Aldehyde Reductase / Q000235:genetics / Q000378:metabolism*; D000074408:Aldo-Keto Reductases; D001483:Base Sequence; D048408:Chlorella vulgaris / Q000235:genetics / Q000378:metabolism; D038181:FMN Reductase; D005415:Flavins / Q000235:genetics; D009243:NAD / Q000235:genetics / Q000378:metabolism; D009249:NADP / Q000235:genetics / Q000378:metabolism; D009930:Organic Chemicals
D005415:Flavins; D009930:Organic Chemicals; D009243:NAD; D009249:NADP; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase; D038181:FMN Reductase; C023903:ferric citrate iron reductase