Chlorella vulgaris aldehyde reductase is capable of functioning as ferric reductase and of driving the fenton reaction in the presence of free flavin

Junichi Sato; Kouji Takeda; Rika Nishiyama; Kouichi Fusayama; Toshiaki Arai; Takumi Sato; Toshihiro Watanabe; Akira Abe; Junichi Nakagawa; Shinji Kawasaki; Youichi Niimura

doi:10.1271/bbb.90798

Chlorella vulgaris aldehyde reductase is capable of functioning as ferric reductase and of driving the fenton reaction in the presence of free flavin

Biosci Biotechnol Biochem. 2010;74(4):854-7. doi: 10.1271/bbb.90798.

Authors

Junichi Sato¹, Kouji Takeda, Rika Nishiyama, Kouichi Fusayama, Toshiaki Arai, Takumi Sato, Toshihiro Watanabe, Akira Abe, Junichi Nakagawa, Shinji Kawasaki, Youichi Niimura

Affiliation

¹ Department of Bioscience, Tokyo University of Agriculture, Japan.

PMID: 20445323
DOI: 10.1271/bbb.90798

Abstract

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.

MeSH terms

Alcohol Oxidoreductases
Aldehyde Reductase / genetics
Aldehyde Reductase / metabolism*
Aldo-Keto Reductases
Base Sequence
Chlorella vulgaris / genetics
Chlorella vulgaris / metabolism
FMN Reductase
Flavins / genetics
NAD / genetics
NAD / metabolism
NADP / genetics
NADP / metabolism
Organic Chemicals

Substances

Flavins
Organic Chemicals
NAD
NADP
Alcohol Oxidoreductases
Aldo-Keto Reductases
Aldehyde Reductase
FMN Reductase
ferric citrate iron reductase