An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase

• Published in: Trends in Biotechnology Vol. 17; no. 6; pp. 244 - 248
• Main Authors: Endo, Isao, Odaka, Masafumi, Yohda, Masafumi
• Format: Book Review Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.06.1999; Elsevier Science
• Subjects: Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Claw setting; Crystal structure; Crystallography, X-Ray; Fundamental and applied biological sciences. Psychology; Hydro-Lyases - chemistry; Hydro-Lyases - physiology; Light; Miscellaneous; Mission oriented research; Nitric oxide; Nitric Oxide - physiology; Nitrile hydratase; Non-heme iron protein; Photoreactivity; Post-translational modification; Rhodococcus - enzymology; Post-translational modification; Biotechnology; Nitric oxide; Nitrile hydratase; Photoreactivity; Biochemistry; Non-heme iron protein; Claw setting; Crystal structure; Photoreactivation; Three dimensional structure; Enzyme; Bacteria; Rhodococcus; Actinomycetes; Lyases; Review; Carbon-oxygen lyases; Hydro-lyases
• ISSN: 0167-7799; 1879-3096
• DOI: 10.1016/S0167-7799(99)01303-7

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.