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

Authors
NOGUCHI T HONDA J NAGAMUNE T SASABE H INOUE Y ENDO I
Citation
T. Noguchi et al., PHOTOSENSITIVE NITRILE HYDRATASE INTRINSICALLY POSSESSES NITRIC-OXIDEBOUND TO THE NONHEME IRON CENTER - EVIDENCE BY FOURIER-TRANSFORM INFRARED-SPECTROSCOPY, FEBS letters, 358(1), 1995, pp. 9-12
Citations number
30
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
358
Issue
1
Year of publication
1995
Pages
9 - 12
Database
ISI
SICI code
0014-5793(1995)358:1<9:PNHIPN>2.0.ZU;2-A
Abstract
Nitrile hydratase (NHase) from Rhodococcus sp, N-771 is a photosensiti ve enzyme that catalyzes hydration of nitriles to the corresponding am ides. Light-induced Fourier transform infrared difference spectra betw een 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 f irst time, that NHase intrinsically possesses nitric oxide (NO) molecu les bound to the non-heme iron center. The possible role of NO in the photoactivation process of NHase is discussed.