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a novel enzymatic system against oxidative stress in the thermophilic hydrogen-oxidizing bacterium hydrogenobacter thermophilus一种新型酶系统对氧化应激的嗜热细菌种氢氧hydrogenobacter酸奶
A Novel Enzymatic System against Oxidative Stress in
the Thermophilic Hydrogen-Oxidizing Bacterium
Hydrogenobacter thermophilus
1 2 1 1 1
Yuya Sato , Masafumi Kameya , Shinya Fushinobu , Takayoshi Wakagi , Hiroyuki Arai ,
Masaharu Ishii1*, Yasuo Igarashi1
1 Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo, Japan, 2 Biotechnology Research Center and Department of Biotechnology, Toyama
Prefectural University, Imizu, Toyama, Japan
Abstract
Rubrerythrin (Rbr) is a non-heme iron protein composed of two distinctive domains and functions as a peroxidase in
anaerobic organisms. A novel Rbr-like protein, ferriperoxin (Fpx), was identified in Hydrogenobacter thermophilus and was
found not to possess the rubredoxin-like domain that is present in typical Rbrs. Although this protein is widely distributed
among aerobic organisms, its function remains unknown. In this study, Fpx exhibited ferredoxin:NADPH oxidoreductase
(FNR)-dependent peroxidase activity and reduced both hydrogen peroxide (H O ) and organic hydroperoxide in the
2 2
presence of NADPH and FNR as electron donors. The calculated Km and Vmax values of Fpx for organic hydroperoxides were
comparable to that for H O , demonstrating a multiple reactivity of Fpx towards hydroperoxides. An fpx gene disruptant
2 2
was unable to grow under aerobic conditions, whereas its growth profiles were comparable to those of the wild-type strain
under anaerobic and microaerobic conditions, clearly indicating the indispensability of Fpx as an antioxidant
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