title: A novel enzymatic system against oxidative stress in the thermophilic hydrogen-oxidizing bacterium Hydrogenobacter thermophilus.
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(2)O(2)) and organic hydroperoxide in the presence of NADPH and FNR as electron donors. The calculated K(m) and V(max) values of Fpx for organic hydroperoxides were comparable to that for H(2)O(2), demonstrating a multiple reactivity of Fpx towards hydroperoxides. An fpx gene disruptant 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 of H. thermophilus in aerobic environments. Structural analysis suggested that domain-swapping occurs in Fpx, and this domain-swapped structure is well conserved among thermophiles, implying the importance of structural stability of domain-swapped conformation for thermal environments. In addition, Fpx was located on a deep branch of the phylogenetic tree of Rbr and Rbr-like proteins. This finding, taken together with the wide distribution of Fpx among Bacteria and Archaea, suggests that Fpx is an ancestral type of Rbr homolog that functions as an essential antioxidant and may be part of an ancestral peroxide-detoxification system.
authors.affiliation: Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
authors.forename: Yuya
authors.initials: Y
authors.lastname: Sato
authors.forename: Masafumi
authors.initials: M
authors.lastname: Kameya
authors.forename: Shinya
authors.initials: S
authors.lastname: Fushinobu
authors.forename: Takayoshi
authors.initials: T
authors.lastname: Wakagi
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Arai
authors.forename: Masaharu
authors.initials: M
authors.lastname: Ishii
authors.forename: Yasuo
authors.initials: Y
authors.lastname: Igarashi
mesh_terms: D001419:Bacteria / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D006859:Hydrogen / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000737:chemistry; D050296:Microbial Viability; D008958:Models, Molecular; D009249:NADP / Q000737:chemistry; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D009195:Peroxidase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D010802:Phylogeny; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D009249:NADP; D006859:Hydrogen; D006861:Hydrogen Peroxide; D009195:Peroxidase