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Updated: Sep 21, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase
1Biochemical Systems Laboratory, The Institute of Physical and Chemical Research (RIKEN), Hirosawa, Wako-shi, Saitama 351-0198, Japan. endo@cel.riken.go.jp
Abstract:
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.
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