Process Optimization of Aldol-Type Reaction by Process Understanding Using in Situ IR

2012 ◽  
Vol 16 (11) ◽  
pp. 1783-1786 ◽  
Author(s):  
Yuki Fukui ◽  
Shinichi Oda ◽  
Hiroyuki Suzuki ◽  
Toshikazu Hakogi ◽  
Daisuke Yamada ◽  
...  
Keyword(s):  
Process Optimization ◽  
Type Reaction ◽  
Process Understanding ◽  
In Situ Ir

In Situ IR Spectroscopy for Following the Copolymerization of CO2and Epoxides

2014 ◽  
Vol 86 (9) ◽  
pp. 1627-1628
Author(s):  
K. Böhm ◽  
W. Leitner ◽  
T. E. Müller
Keyword(s):  
Ir Spectroscopy ◽  
In Situ Ir ◽  
In Situ Ir Spectroscopy

In situ IR observation of photo-chemically deposited silicon nitride thin films

1991 ◽  
Vol 48-49 ◽  
pp. 409-413 ◽  
Author(s):  
T. Wadayama ◽  
T. Hihara ◽  
A. Hatta ◽  
W. Suëtaka
Keyword(s):  
Thin Films ◽  
Silicon Nitride ◽  
In Situ Ir

scholarly journals In Situ IR Spectroscopy of Mesoporous Silica Films for Monitoring Adsorption Processes and Trace Analysis

2018 ◽  
Vol 1 (12) ◽  
pp. 7083-7091 ◽  
Author(s):  
Bettina Baumgartner ◽  
Jakob Hayden ◽  
Andreas Schwaighofer ◽  
Bernhard Lendl
Keyword(s):  
Ir Spectroscopy ◽  
Mesoporous Silica ◽  
Trace Analysis ◽  
Silica Films ◽  
In Situ Ir ◽  
Adsorption Processes ◽  
In Situ Ir Spectroscopy

scholarly journals How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer

2019 ◽  
Author(s):  
Moritz Senger ◽  
Viktor Eichmann ◽  
Konstantin Laun ◽  
Jifu Duan ◽  
Florian Wittkamp ◽  
...  
Keyword(s):  
Amino Acid ◽  
Proton Transfer ◽  
Active Site ◽  
Molecular Hydrogen ◽  
H2 Production ◽  
Amino Acid Residues ◽  
Difference Spectroscopy ◽  
Dynamic Changes ◽  
In Situ Ir

Hydrogenases are metalloenzymes that catalyse the interconversion of protons and molecular hydrogen, H2. [FeFe]-hydrogenases show particularly high rates of hydrogen turnover and have inspired numerous compounds for biomimetic H2 production. Two decades of research on the active site cofactor of [FeFe]-hydrogenases have put forward multiple models of the catalytic proceedings. In comparison, understanding of the catalytic proton transfer is poor. We were able to identify the amino acid residues forming a proton transfer pathway between active site cofactor and bulk solvent; however, the exact mechanism of catalytic proton transfer remained inconclusive. Here, we employ in situ IR difference spectroscopy on the [FeFe]-hydrogenase from Chlamydomonas reinhardtii evaluating dynamic changes in the hydrogen-bonding network upon catalytic proton transfer. Our analysis allows for a direct, molecular unique assignment to individual amino acid residues. We found that transient protonation changes of arginine and glutamic acid residues facilitate bidirectional proton transfer in [FeFe]-hydrogenases.<br>

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