1.
Oxygen saturation and electromyographic changes in masseter muscle during experimental chewing of gum with harder texture.
Horikoshi, E, Ishikawa, H, Yoshida, T, Tamaoki, S, Kajii, TS
Acta odontologica Scandinavica. 2013;(6):1378-85
Abstract
OBJECTIVE The purpose of this study was to clarify the relationship between changes in masseter muscle oxygenation measured by near-infrared spectroscopy (NIRS) and changes in the electromyographic (EMG) power spectrum during experimental chewing of gum with harder texture, to improve the understanding of the use of NIRS in assessing masseter muscle fatigue. MATERIAL AND METHODS Ten female volunteers with normal occlusion were examined. Mean age (standard deviation) was 28.4 (3.8) years. Mean fracture stress of gum was 12.5 × 10(4) N/m(2). Subjects were instructed to chew gum for 60 s (75 strokes) on the voluntary chewing side at a pace of 1.25 strokes/s. Simultaneous recordings of NIRS and EMG signals from masseter muscle were performed during gum chewing. RESULTS Oxygen saturation levels decreased from the start of chewing, then stabilized with a break point between the two phases. The normalized EMG amplitude increased and the mean frequency of the EMG power spectrum decreased during gum chewing. The timing of break point appearance was related to the timing of a significant decrease in median frequency, but no clear relationships were found between break point appearance and increased EMG amplitude. CONCLUSIONS These results suggest that the break point of the oxygen saturation curve, as obtained from NIRS measurements, could be used as an indicator of masseter muscle fatigue as assessed by a shift in the EMG power spectrum to lower frequencies.
2.
Structural dynamics of proximal heme pocket in HemAT-Bs associated with oxygen dissociation.
Yoshida, Y, Ishikawa, H, Aono, S, Mizutani, Y
Biochimica et biophysica acta. 2012;(7):866-72
Abstract
HemAT from Bacillus subtilis (HemAT-Bs) is a heme-containing O(2) sensor protein that acts as a chemotactic signal transducer. Binding of O(2) to the heme in the sensor domain of HemAT-Bs induces a conformational change in the protein matrix, and this is transmitted to a signaling domain. To characterize the specific mechanism of O(2)-dependent conformational changes in HemAT-Bs, we investigated time-resolved resonance Raman spectra of the truncated sensor domain and the full-length HemAT-Bs upon O(2) and CO dissociation. A comparison between the O(2) and CO complexes provides insights on O(2)/CO discrimination in HemAT-Bs. While no spectral changes upon CO dissociation were observed in our experimental time window between 10ns and 100μs, the band position of the stretching mode between the heme iron and the proximal histidine, ν(Fe-His), for the O(2)-dissociated HemAT-Bs was lower than that for the deoxy form on time-resolved resonance Raman spectra. This spectral change specific to O(2) dissociation would be associated with the O(2)/CO discrimination in HemAT-Bs. We also compared the results obtained for the truncated sensor domain and the full-length HemAT-Bs, which showed that the structural dynamics related to O(2) dissociation for the full-length HemAT-Bs are faster than those for the sensor domain HemAT-Bs. This indicates that the heme proximal structural dynamics upon O(2) dissociation are coupled with signal transduction in HemAT-Bs.