Photosensitivity of the Ni-A state of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F with visible light

• Osuka, Hisao

• Shomura, Yasuhito

• Komori, Hirofumi

• Shibata, Naoki

• Nagao, Satoshi

• Higuchi, Yoshiki

• Hirota, Shun

抄録

[NiFe] hydrogenase catalyzes reversible oxidation of molecular hydrogen. Its active site is constructed of a hetero dinuclear Ni-Fe complex, and the oxidation state of the Ni ion changes according to the redox state of the enzyme. We found that the Ni-A state (an inactive unready, oxidized state) of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F (DvMF) is light sensitive and forms a new state (Ni-AL) with irradiation of visible light. The Fourier transform infrared (FT-IR) bands at 1956, 2084 and 2094 cm^-1 of the Ni-A state shifted to 1971, 2086 and 2098 cm^-1 in the Ni-AL state. The g-values of gx = 2.30, gy = 2.23 and gz = 2.01 for the signals in the electron paramagnetic resonance (EPR) spectrum of the Ni-A state at room temperature varied for -0.009, +0.012 and +0.010, respectively, upon light irradiation. The light-induced Ni-AL state converted back immediately to the Ni-A state under dark condition at room temperature. These results show that the coordination structure of the Fe site of the Ni-A state of [NiFe] hydrogenase is perturbed significantly by light irradiation with relatively small coordination change at the Ni site.

収録刊行物

• Biochemical and Biophysical Research Communications

  Biochemical and Biophysical Research Communications 430 (1), 284-288, 2013-01-04

  Elsevier

キーワード

• [NiFe] hydrogenase
• Desulfovibrio vulgaris Miyazaki F
• Ni-A state
• Light sensitivity
• FT-IR
• EPR

詳細情報

• CRID: 1050014359399323008
• NII論文ID: 120005716864
• NII書誌ID: AA00564395
• ISSN: 0006291X
• HANDLE: 10061/10416
• Web Site: https://naist.repo.nii.ac.jp/records/9685
• 本文言語コード: en
• 資料種別: journal article
• データソース種別:
  • IRDB
  • CiNii Articles