Highly efficient control of iron‐containing nitrile hydratases by stoichiometric amounts of nitric oxide and light

FEBS Letters

Pétré, Dominique¹  Mansuy, Daniel²  Moali, Catherine²  Artaud, Isabelle²  Bonnet, Didier² 

[1] Laboratoire de Catalyse Enzymatique, Rhône-Poulenc Recherches, Centre des Carrières, 85 avenue des Frères Perret 69192 Saint-Fons Cédex, France;Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques (URA 400 CNRS), Université Paris V, 45 rue des St. Pères 75270 Paris Cédex 06, France

关键词: Rhodococcus sp. R312 or BR312;    Comamonas testosteroni NI1;    Charge transfer band;    Fe–NO bond;    NHase;    nitrile hydratase;    EPR;    electron paramagnetic resonance;    FTIR;    Fourier transform infrared;    rbNOS;    rat brain nitric oxide synthase;    HbFeIII;    methemoglobin;    HbO2;    oxyhemoglobin;   

DOI  :  10.1016/S0014-5793(97)00511-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The reaction of two iron-containing nitrile hydratases (NHase) with NO has been studied: NHase from Rhodococcus sp. R312, which is probably similar to the photosensitive N771 NHase, and the new NHase from Comamonas testosteroni NI1 whose aminoacid sequence is quite different from those of BR312 and N771 NHases. Both enzymes are equally inactivated after addition of stoichiometric amounts of NO added as an anaerobic solution or produced in situ under physiological conditions by a rat brain NO-synthase. Both enzymes are reactivated by photoirradiation, and two cycles of NO inactivation/photoactivation can be performed without significant loss of activity. Both iron-containing NHases have a high affinity for NO, similar to that of methemoglobin.

【 授权许可】

Unknown