Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non-heme iron center: evidence by Fourier transform infrared spectroscopy.
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 (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.
Noguchi
T
T
Solar Energy Research Group, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
Honda
J
J
Nagamune
T
T
Sasabe
H
H
Inoue
Y
Y
Endo
I
I
D004789:Enzyme Activation; D006836:Hydro-Lyases / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D008027:Light; D009569:Nitric Oxide / Q000737:chemistry*; D012240:Rhodococcus / Q000201:enzymology*; D017550:Spectroscopy, Fourier Transform Infrared
D009569:Nitric Oxide; D007501:Iron; D006836:Hydro-Lyases; C048831:nitrile hydratase