An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase.
Extensive studies have revealed the molecular mechanism of the photoreactivity of nitrile hydratase from Rhodococcus sp. N-771. In the inactive enzyme, nitric oxide is bound to the non-heme ferric iron at the catalytic center, stabilized by a claw-like structure formed by two post-translationally modified cysteines and a serine. The inactive nitrile hydratase is activated by the photoinduced release of the nitric oxide. This result might provide a means of designing novel photoreactive chemical compounds or proteins that would be applicable to biochips and light-controlled metabolic systems.
Endo
I
I
Biochemical Systems Laboratory, The Institute of Physical and Chemical Research (RIKEN), Hirosawa, Wako-shi, Saitama 351-0198, Japan. endo@cel.riken.go.jp
Odaka
M
M
Yohda
M
M
D018360:Crystallography, X-Ray; D006836:Hydro-Lyases / Q000737:chemistry / Q000502:physiology*; D008027:Light; D009569:Nitric Oxide / Q000502:physiology; D012240:Rhodococcus / Q000201:enzymology*
D009569:Nitric Oxide; D006836:Hydro-Lyases; C048831:nitrile hydratase