Is H[sub 2]O[sub 2] Involved in the Membrane Degradation Mechanism in PEMFC?

2006 ◽  
Vol 9 (6) ◽  
pp. A299 ◽  
Author(s):  
Vishal O. Mittal ◽  
H. Russell Kunz ◽  
James M. Fenton
2008 ◽  
Vol 155 (1) ◽  
pp. A29 ◽  
Author(s):  
Satoru Hommura ◽  
Kengo Kawahara ◽  
Tetsuji Shimohira ◽  
Yasutake Teraoka

2008 ◽  
Vol 182 (1) ◽  
pp. 39-47 ◽  
Author(s):  
Atsushi Ohma ◽  
Shinji Yamamoto ◽  
Kazuhiko Shinohara

Author(s):  
Yuuki Okano ◽  
Masato Ooishi ◽  
Atsushi Ohma ◽  
Kazuyoshi Fushinobu ◽  
Ken Okazaki

Potential distribution in the electrolyte membrane in the MEA of PEFC has been measured in order to help understand a recently suggested membrane degradation mechanism caused by Pt band. A thin metallic probe, Pt or Au, is inserted in membrane to measure the potential distribution. The measured profile shows abrupt change at certain position, and the position is influenced by the operation and cell design parameters. A simple theoretical model to predict the potential distribution is developed and showed good agreement with experimental results.


2019 ◽  
Vol 476 (21) ◽  
pp. 3333-3353 ◽  
Author(s):  
Malti Yadav ◽  
Kamalendu Pal ◽  
Udayaditya Sen

Cyclic dinucleotides (CDNs) have emerged as the central molecules that aid bacteria to adapt and thrive in changing environmental conditions. Therefore, tight regulation of intracellular CDN concentration by counteracting the action of dinucleotide cyclases and phosphodiesterases (PDEs) is critical. Here, we demonstrate that a putative stand-alone EAL domain PDE from Vibrio cholerae (VcEAL) is capable to degrade both the second messenger c-di-GMP and hybrid 3′3′-cyclic GMP–AMP (cGAMP). To unveil their degradation mechanism, we have determined high-resolution crystal structures of VcEAL with Ca2+, c-di-GMP-Ca2+, 5′-pGpG-Ca2+ and cGAMP-Ca2+, the latter provides the first structural basis of cGAMP hydrolysis. Structural studies reveal a typical triosephosphate isomerase barrel-fold with substrate c-di-GMP/cGAMP bound in an extended conformation. Highly conserved residues specifically bind the guanine base of c-di-GMP/cGAMP in the G2 site while the semi-conserved nature of residues at the G1 site could act as a specificity determinant. Two metal ions, co-ordinated with six stubbornly conserved residues and two non-bridging scissile phosphate oxygens of c-di-GMP/cGAMP, activate a water molecule for an in-line attack on the phosphodiester bond, supporting two-metal ion-based catalytic mechanism. PDE activity and biofilm assays of several prudently designed mutants collectively demonstrate that VcEAL active site is charge and size optimized. Intriguingly, in VcEAL-5′-pGpG-Ca2+ structure, β5–α5 loop adopts a novel conformation that along with conserved E131 creates a new metal-binding site. This novel conformation along with several subtle changes in the active site designate VcEAL-5′-pGpG-Ca2+ structure quite different from other 5′-pGpG bound structures reported earlier.


Proceedings ◽  
2020 ◽  
Vol 1 (1) ◽  
Author(s):  
Youssra El Qasemy ◽  
Abdelfatah Achahbar ◽  
Abdellatif Khamlichi

The stochastic behavior of wind speed is a particular characteristic of wind energy production, which affects the degradation mechanism of the turbine, resulting in stochastic charging on the wind turbine. A model stochastic is used in this study to evaluate the efficiency of wind turbine power of whatever degree given fluctuating wind turbulence data. This model is based on the Langevin equations, which characterize, by two coefficients, drift and diffusion functions. These coefficients describe the behavior of the transformation process from the input wind speed to the output data that need to be determined. For this present work, the computation of drift and diffusion functions has been carried out by using the stochastic model to assess the output variables in terms of the torque and power curves as a function of time, and it is compared by the classical method. The results show that the model stochastic can define the efficiency of wind turbine generation more precisely.


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