Effect of Current Distribution on Quartz Crystal Microbalance Measurements

1998 ◽  
Vol 145 (2) ◽  
pp. 492-497 ◽  
Author(s):  
James J. Kelly ◽  
K. M. Anisur Rahman ◽  
Christopher J. Durning ◽  
Alan C. West
1997 ◽  
Vol 502 ◽  
Author(s):  
James J. Kelly ◽  
Christopher J. Durning ◽  
Alan C. West

ABSTRACTSpatially nonuniform electrodeposition can cause discrepancies between predicted and experimentally measured mass loadings on an electrochemical quartz crystal microbalance (EQCM) since the sensitivity of the quartz crystal varies significantly from point to point. These discrepancies can be significant even if the current distribution is nearly uniform. These effects were examined experimentally by varying the conductivity of the electrolyte and the current density during the electrodeposition of copper on an EQCM, effecting changes in the spatial, deposited-mass distribution in a controlled manner. The resulting frequency shifts are in agreement with results predicted by current distribution simulations, validated a posteriori with profilometry measurements. Our results permit determination of the spatial variation of the quartz crystal sensitivity factor or of the current distribution on the EQCM.


2019 ◽  
Vol 25 (6) ◽  
pp. 879-884
Author(s):  
Takahiro Sakai ◽  
Hayato Seki ◽  
Shogo Yoshida ◽  
Hayato Hori ◽  
Hisashi Suzuki ◽  
...  

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sin-Cih Sun ◽  
Hung-Wei Huang ◽  
Yi-Ting Lo ◽  
Min-Chieh Chuang ◽  
Yuan-Hao Howard Hsu

AbstractCardiolipin (CL), a crucial component in inner mitochondrial membranes, interacts with cytochrome c (cyt c) to form a peroxidase complex for the catalysis of CL oxidation. Such interaction is pivotal to the mitochondrial regulation of apoptosis and is affected by the redox state of cyt c. In the present study, the redox-dependent interaction of cyt c with CL was investigated through amide hydrogen/deuterium exchange coupled with mass spectrometry (HDXMS) and quartz crystal microbalance with dissipation monitoring (QCM-D). Ferrous cyt c exhibited a more compact conformation compared with its ferric form, which was supported by the lower number of deuterons accumulated and the greater amplitude reduction on dissipation. Upon association with CL, ferrous cyt c resulted in a moderate increase in deuteration, whereas the ferric form caused a drastic increase of deuteration, which indicated that CL-bound ferric cyt c formed an extended conformation. These results were consistent with those of the frequency (f) − dissipation (D) experiments, which revealed that ferric cyt c yielded greater values of |ΔD/Δf| within the first minute. Further fragmentation analysis based on HDXMS indicated that the effect of CL binding was considerably different on ferric and ferrous cyt c in the C-helix and the Loop 9–24. In ferric cyt c, CL binding affected Met80 and destabilized His18 interaction with heme, which was not observed with ferrous cyt c. An interaction model was proposed to explain the aforementioned results.


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