Electromyographic evaluation of the masseter and temporal muscles activity in volunteers submitted to acupuncture.

AIM: To assess the effect of acupuncture on the temporal and masseter muscles activity employing surface electromyography. METHODS: Thirty volunteers were evaluated according to three groups of acupuncture application: selected local points, selected points at distance and association of local and distant points. Bipolar surface electrodes were positioned bilaterally on the anterior portion of temporal muscle, as well as in the median region of masseter muscle. An electromyograph connected to a computer and a specific software registered the muscular activity before and after acupuncture, in the following experimental conditions: 1- Rest Position (RP); 2- Maximum Intercuspation Clenching (MIC); 3- Bilateral Molar Clenching with Cotton Rolls (BMCCR). The mean values obtained for the activities of the studied muscles were submitted to Analysis of Variance and Tukey complementary test. RESULTS: The electromyographic activity of the studied muscles was lower after the application of the methods of acupuncture in the Rest, and higher after the application of the acupuncture in the Maximum Intercuspation Clenching; the electromyographic activity of the temporal muscle was higher than the masseter muscle in the Rest and lower in the Bilateral molar clenching with cotton rolls; the electromyographic activity showed to be modified after the three used methods of acupuncture in the Maximum Intercuspation Clenching. In this clinical condition, the method of long-distance acupuncture was higher than the application of local needles and the associated method. CONCLUSION: Acupuncture provided alterations in the activity of the studied muscles, favoring conditions of rest and muscular tightness.

New inhibitors of iron-containing nitrile hydratases.

There is growing evidence in the literature emphasizing the significance of the post-translational modification of cysteine thiols to sulfenic acids (SOH), which have been found in a number of proteins. Crystallographic and mass spectrometric evidence has shown the presence of this group in an inactive form of the industrially important enzyme nitrile hydratase (NHase). This oxidized cysteine is unique in that it forms part of the coordination sphere of the low-spin iron III at the active site of the enzyme. The presence of this unstable sulfenic group in the active form of NHase is the subject of some controversy. To try to detect this function in NHase, we have studied the inhibitory effect on nitrile hydration of reagents known to react with sulfenic acids. Two NHases were studied, namely, Rhodococcus rhodochrous R312 NHase and Comamonas testosteroni NI1 NHase, and the reagents used were meta-chlorocarbonyldicyano-phenylhydrazone (m-ClCP), 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl), and 2-nitro-5-thiocyanato-benzoic acid (NTBA). Following this approach we report three novel inhibitors of NHases. In addition, we report thiocyanate reagents that can be used to monitor NHase activity spectroscopically.

Clean oxidation of thiolates to sulfinates in a four-coordinate CoIII complex with a mixed carboxamido N-thiolato S donor set: relevance to nitrile hydratase.

A new [Co(N2(SO2)2)(CNtBu)2](Et4N) complex 6 was prepared from N,N'-(3-mercapto-3-methyl-butyryl)-o-phenylenediamine and completely characterized. While the starting square planar complex [Co(N2S2)](Et4N) 4 was destroyed by dioxirane, the Co ligated thiolates of the six-coordinate intermediate [Co(N2S2)(CNtBu)2](Et4N) complex 5 was readily oxidized to sulfinates with a stoichiometric amount of this oxidant. The resulting complex 6 crystallizes with an octahedral structure. The SO bonds of the SO2 groups are almost equivalent (approximately 1.483 and approximately 1.453 A). The isonitrile is linearly bonded to the cobalt with a Co-C-N angle of 177.5 degrees and a very short C-N(tBu) distance of 1.13 A, which has a triple bond character. As expected for six-coordinate CoIII complexes, 5 and 6 are diamagnetic in agreement with their 1H and 13C NMR spectra. The SO2 IR bands are located at 1210 cm(-1) (v(as)SO2) and 1070 cm(-1) (v(s)SO2), while the CN vibration of the isonitrile is observed at 2170 cm(-1) in 5 and 2210 cm(-1) in 6. Very recently, it has been reported in the literature that oxidation of the coordinated thiolates was required for activity of both Fe and Co nitrile hydratases. Complex 6, with two oxidized thiolates trans to two deprotonated carboxamido nitrogens, is the first to have an in-plane closely related to that of the Co-NHase active site.