Desulforubrerythrin from Campylobacter jejuni, a novel multidomain protein

被引:13
|
作者
Pinto, Ana F. [1 ]
Todorovic, Smilja [1 ]
Hildebrandt, Peter [2 ]
Yamazaki, Manabu [3 ]
Amano, Fumio [4 ]
Igimi, Shizunobu [3 ]
Romao, Celia V. [1 ]
Teixeira, Miguel [1 ]
机构
[1] Univ Nova Lisboa, Inst Tecnol Quim & Biol, P-2780157 Oeiras, Portugal
[2] Tech Univ Berlin, Inst Chem, D-10623 Berlin, Germany
[3] Natl Inst Hlth Sci, Setagaya Ku, Tokyo 1588501, Japan
[4] Osaka Univ Pharmaceut Sci, Osaka 5691094, Japan
来源
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2011年 / 16卷 / 03期
关键词
Rubrerythrin; Hydrogen peroxide; Rubredoxin; Electron paramagnetic resonance; Resonance Raman spectroscopy; NONHEME IRON PROTEIN; DESULFOVIBRIO-VULGARIS RUBRERYTHRIN; SULFOLOBUS-TOKODAII STRAIN-7; ESCHERICHIA-COLI; SPECTROSCOPIC PROPERTIES; ARCHAEOGLOBUS-FULGIDUS; RESPIRATORY OXIDASES; SUPEROXIDE-DISMUTASE; PYROCOCCUS-FURIOSUS; CRYSTAL-STRUCTURE;
D O I
10.1007/s00775-010-0749-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A novel multidomain metalloprotein from Campylobacter jejuni was overexpressed in Escherichia coli, purified, and extensively characterized. This protein is isolated as a homotetramer of 24-kDa monomers. According to the amino acid sequence, each monomer was predicted to contain three structural domains: an N-terminal desulforedoxin-like domain, followed by a four-helix bundle domain harboring a non-sulfur mu-oxo diiron center, and a rubredoxin-like domain at the C-terminus. The three predicted iron sites were shown to be present and were studied by a combination of UV-vis, EPR, and resonance Raman spectroscopies, which allowed the determination of the electronic and redox properties of each site. The protein contains two FeCys(4) centers with reduction potentials of +240 mV (desulforedoxin-like center) and +185 mV (rubredoxin-like center). These centers are in the high-spin configuration in the as-isolated ferric form. The protein further accommodates a mu-oxo-bridged diiron site with reduction potentials of +270 and +235 mV for the two sequential redox transitions. The protein is rapidly reoxidized by hydrogen peroxide and has a significant NADH-linked hydrogen peroxide reductase activity of 1.8 mu mol H2O2 min(-1) mg(-1). Owing to its building blocks and its homology to the rubrerythrin family, the protein is named desulforubrerythrin. It represents a novel example of the large diversity of the organization of domains exhibited by this enzyme family.
引用
收藏
页码:501 / 510
页数:10
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