PHOTOSENSITIVE NITRILE HYDRATASE INTRINSICALLY POSSESSES NITRIC-OXIDE BOUND TO THE NONHEME IRON CENTER - EVIDENCE BY FOURIER-TRANSFORM INFRARED-SPECTROSCOPY

被引:88
作者
NOGUCHI, T
HONDA, J
NAGAMUNE, T
SASABE, H
INOUE, Y
ENDO, I
机构
[1] RIKEN,FRONTIER RES PROGRAM,WAKO,SAITAMA 35101,JAPAN
[2] UNIV TOKYO,FAC ENGN,BUNKYO KU,TOKYO 113,JAPAN
[3] RIKEN,CHEM ENGN LAB,WAKO,SAITAMA 35101,JAPAN
关键词
NITRIC OXIDE; NITRILE HYDRATASE; FOURIER TRANSFORM INFRARED SPECTROSCOPY; NONHEME IRON; PHOTOACTIVATION;
D O I
10.1016/0014-5793(94)01374-A
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
Nitrile hydratase (NHase) from Rhodococcus sp, N-771 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 (N-14) and N-15-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.
引用
收藏
页码:9 / 12
页数:4
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