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Highly efficient control of iron‐containing nitrile hydratases by stoichiometric amounts of nitric oxide and light
Author(s) -
Bonnet Didier,
Artaud Isabelle,
Moali Catherine,
Pétré Dominique,
Mansuy Daniel
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00511-5
Subject(s) - nitrile hydratase , comamonas testosteroni , chemistry , methemoglobin , nitrile , enzyme , rhodococcus rhodochrous , biochemistry , rhodococcus , stoichiometry , hemoglobin , organic chemistry
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.