Catalytic oxidation plays a crucial role in chemical industry,in which the utilization of abundant and environmental-friendly oxygen(O_(2))as oxidant aligns with sustainable development principles in green chemistry.H...Catalytic oxidation plays a crucial role in chemical industry,in which the utilization of abundant and environmental-friendly oxygen(O_(2))as oxidant aligns with sustainable development principles in green chemistry.However,the intrinsic inertness of ground-state O_(2) molecule poses a long-standing challenge in developing an efficient non-noble metal-based catalyst.Herein,inspired by the electron transfer process in respiratory chain,we engineered long-range N_(V) to mediate Fe_(1) center for O_(2) activation in aerobic oxidation.Combined in/quasi-situ spectroscopic characterizations and control experiments suggest the Fe_(1) site efficiently adsorbs O_(2),and the N_(V) site facilitates electron delocalization to adjacent Fe_(1),providing efficient transformation of O_(2) to reactive oxygen species that boost oxidation reactions mildly.This Fe_(1)--N_(V) single-atom catalyst demonstrates outstanding catalytic performance in aerobic oxidations of alkanes,N-heterocycles,alcohols,and amines under relatively mild conditions.Our findings offer a new perspective for designing high-efficiency heterogeneous catalysts in aerobic oxidations,promising various potential applications.展开更多
Objective:To investigate the membrane localization function of the CX26 protein when its 86th amino acid is Thr, Ser or Arg, and its relations to deafness. Methods:CX26-GFP protein with either Thr, Ser or Arg as the 8...Objective:To investigate the membrane localization function of the CX26 protein when its 86th amino acid is Thr, Ser or Arg, and its relations to deafness. Methods:CX26-GFP protein with either Thr, Ser or Arg as the 86th amino acid was expressed in mouse SGN cells via the GFP fusion type lenti-virus expression system. The membrane localization of the fusion protein was observed under a fluorescence microscope. Results:The mutated protein of CX26 T86S was localized to cell membrane and form gap conjunction structures, showing no difference to the wild type CX26 protein (with Thr as the 86th amino acid). However, the gap conjunction structure disappeared when the mutation was CX26 T86A. Conclusion:These results indicate that the CX26 T86R mutation may be a cause of hearing loss, but CX26 T86S as a non-pathogenic poly-morphism mutation does not affect functions of the CX26 protein. The results are in accordance with the results of clinical screening.展开更多
Occupants’thermal comfort in buildings may be affected by the cool wall and warm wall,which is attributed to the effect of asymmetric radiation.However,the previous majority of the researches on asymmetric radiation ...Occupants’thermal comfort in buildings may be affected by the cool wall and warm wall,which is attributed to the effect of asymmetric radiation.However,the previous majority of the researches on asymmetric radiation were mainly about the comfort limits under thermally neutral condition within 1∼1.5 h but had not considered the effect of exposure duration and the condition beyond neutral.To investigate the human thermal comfort under an asymmetric environment caused by the cool wall and warm wall,forty-four subjects were exposed to neutral air temperature with lateral radiant asymmetries in winter and summer for 3 h.The results indicated that the cool wall caused thermal discomfort easier than the warm wall because the thermal sensation decreased and deviated from neutral with time.Subjects’sensitivity of local parts to asymmetric radiation was affected in the conditions beyond neutral,thus their acceptability to asymmetric radiation decreased.The currently used limits of radiant temperature asymmetry tended to underestimate the local discomfort due to the walls.For the conditions tested,The limits of 5%dissatisfaction in radiant temperature asymmetry were 4.4°C(180 min)and 1.8°C(60 min and 120 min)for the warm wall,and 1.8°C at 60 min for the cool wall.展开更多
文摘Catalytic oxidation plays a crucial role in chemical industry,in which the utilization of abundant and environmental-friendly oxygen(O_(2))as oxidant aligns with sustainable development principles in green chemistry.However,the intrinsic inertness of ground-state O_(2) molecule poses a long-standing challenge in developing an efficient non-noble metal-based catalyst.Herein,inspired by the electron transfer process in respiratory chain,we engineered long-range N_(V) to mediate Fe_(1) center for O_(2) activation in aerobic oxidation.Combined in/quasi-situ spectroscopic characterizations and control experiments suggest the Fe_(1) site efficiently adsorbs O_(2),and the N_(V) site facilitates electron delocalization to adjacent Fe_(1),providing efficient transformation of O_(2) to reactive oxygen species that boost oxidation reactions mildly.This Fe_(1)--N_(V) single-atom catalyst demonstrates outstanding catalytic performance in aerobic oxidations of alkanes,N-heterocycles,alcohols,and amines under relatively mild conditions.Our findings offer a new perspective for designing high-efficiency heterogeneous catalysts in aerobic oxidations,promising various potential applications.
基金supported by grants from the National Basic Research Program of China (973 Program) (#2012CB967900)National Natural Science Foundation of China (31300624, 81470684)+3 种基金Postdoctoral Science Foundation of China (2015M571818)Six Major Categories Talent (2014-WSN043, 2011-WS-074)Innovation and Entrepreneurship Training Program for College Students in Jiangsu Province (201510313003Z, 201510313003, KYLX14-1455)Clinic Medical Special Foundation of Jiangsu province (b12014032)
文摘Objective:To investigate the membrane localization function of the CX26 protein when its 86th amino acid is Thr, Ser or Arg, and its relations to deafness. Methods:CX26-GFP protein with either Thr, Ser or Arg as the 86th amino acid was expressed in mouse SGN cells via the GFP fusion type lenti-virus expression system. The membrane localization of the fusion protein was observed under a fluorescence microscope. Results:The mutated protein of CX26 T86S was localized to cell membrane and form gap conjunction structures, showing no difference to the wild type CX26 protein (with Thr as the 86th amino acid). However, the gap conjunction structure disappeared when the mutation was CX26 T86A. Conclusion:These results indicate that the CX26 T86R mutation may be a cause of hearing loss, but CX26 T86S as a non-pathogenic poly-morphism mutation does not affect functions of the CX26 protein. The results are in accordance with the results of clinical screening.
基金The work was supported by"The 13th Five-Year"National Key R&D Program of China(2018YFC0704500)the National Natural Science Foundation of China under Grant No.51778439.
文摘Occupants’thermal comfort in buildings may be affected by the cool wall and warm wall,which is attributed to the effect of asymmetric radiation.However,the previous majority of the researches on asymmetric radiation were mainly about the comfort limits under thermally neutral condition within 1∼1.5 h but had not considered the effect of exposure duration and the condition beyond neutral.To investigate the human thermal comfort under an asymmetric environment caused by the cool wall and warm wall,forty-four subjects were exposed to neutral air temperature with lateral radiant asymmetries in winter and summer for 3 h.The results indicated that the cool wall caused thermal discomfort easier than the warm wall because the thermal sensation decreased and deviated from neutral with time.Subjects’sensitivity of local parts to asymmetric radiation was affected in the conditions beyond neutral,thus their acceptability to asymmetric radiation decreased.The currently used limits of radiant temperature asymmetry tended to underestimate the local discomfort due to the walls.For the conditions tested,The limits of 5%dissatisfaction in radiant temperature asymmetry were 4.4°C(180 min)and 1.8°C(60 min and 120 min)for the warm wall,and 1.8°C at 60 min for the cool wall.
