Formate dehydrogenase (FDH) is a D-2-hydroxy acid dehydrogenase, which can reversibly reduce CO2 to formate and thus act as non-photosynthetic CO2 reductase. In order to increase catalytic efficiency of formate dehydrogenase for CO2 reduction, the formate dehydrogenase CbFDHM2 was used as the parent to conduct single-site saturation and iterative combinatorial mutagenesis, and two mutants V328I/F285W and V354G/F285W were obtained of which reduction activity was about two times more than the CbFDHM2 and had greater potential in CO2 reduction. The optimal temperature for V328I/F285W and V354G/F285W was 55℃, and the optimal pH was 9.0. Then the molecular basis for its improvement of biochemical characteristics were preliminarily elucidated by computer-aided methods. All of these results further established a solid foundation for molecular modification of formate dehydrogenase and CO2 reduction.
Propagation of guided electron waves in two coupled quantum wells is studied and analyzed by decomposing 1-D coupled eigenstates in terms of multiple eigenstates of individual wells. The energy transfer from one mode to the other modes in either channel is characterized. The dominant transfer is to the matched mode in the other channel. But tunneling to other modes nearest in energy to the incident mode is found to be quite large, I)altidularly under high mode injection.(4) When the electron energy E is less than a certain eigenvalue E, the wave vectors for those subbands with minima above this energy become imaginary, resulting in evanescent inodes. As the evanescent modes decay exponentially, SPIE Vol. 1675 Quantum WellandSuperlattice Physics IV(1992)/343 Downloaded From: http://proceedings.spiedigitallibrary.org/ on 06/15/2016 Terms of Use: http://spiedigitallibrary.org/ss/TermsOfUse.aspx
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