Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non‐heme iron center: evidence by Fourier transform infrared spectroscopy

FEBS Letters

Nagamune, Teruyuki¹  Sasabe, Hiroyuki³  Endo, Isao²  Inoue, Yorinao⁴  Honda, Jun³  Noguchi, Takumi⁴ 

[1] Faculty of Engineering, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan;Chemical Engineering Laboratory, RIKEN, Saitama, Japan;Frontier Research Program, RIKEN, Saitama, Japan;Solar Energy Research Group, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01, Japan

关键词: Nitric oxide;    Nitrile hydratase;    Fourier transform infrared spectroscopy;    Non-heme iron;    Photoactivation;    ENDOR;    electron nuclear double resonance;    EPR;    electron paramagnetic resonance;    EXAFS;    extended X-ray absorption fine structure;    FTIR;    Fourier transform infrared;    NHase;    nitrite hydratase;    NOS;    nitrite oxide synthase;   

DOI  :  10.1016/0014-5793(94)01374-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a photosensitive enzyme that catalyzes hydration of nitriles to the corresponding amides. Light-induced Fourier transform infrared difference spectra between the inactive and active forms of NHase were measured with both the natural (¹⁴N) and ¹⁵N-labeled NHases. The results showed, for the first time, that NHase intrinsically possesses nitric oxide (NO) molecules bound to the non-heme iron center. The possible role of NO in the photoactivation process of NHase is discussed.

【 授权许可】

Unknown