通过化学计量的一氧化氮和光对含铁腈水合酶进行高效控制。

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

作者信息

Bonnet D, Artaud I, Moali C, Pétré D, Mansuy D

机构信息

Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques (URA 400 CNRS), Université Paris V, France.

出版信息

FEBS Lett. 1997 Jun 9;409(2):216-20. doi: 10.1016/s0014-5793(97)00511-5.

DOI:10.1016/s0014-5793(97)00511-5

PMID:9202148

Abstract

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.

摘要

对两种含铁腈水合酶（NHase）与一氧化氮（NO）的反应进行了研究：来自红球菌属R312的NHase，其可能与光敏N771 NHase相似；以及来自睾丸酮丛毛单胞菌NI1的新型NHase，其氨基酸序列与BR312和N771 NHase的氨基酸序列有很大不同。当加入化学计量的NO（以厌氧溶液形式添加或在生理条件下由大鼠脑一氧化氮合酶原位产生）后，两种酶均被同等程度地灭活。两种酶均可通过光照射重新激活，并且可以进行两个周期的NO灭活/光激活而不会有明显的活性损失。两种含铁NHase对NO都具有高亲和力，类似于高铁血红蛋白。