Electrochemical Study of Reversible Hydrogenase Reaction ofDesulfovibrio vulgarisCells with Methyl Viologen as an Electron Carrier

1999 ◽  
Vol 71 (9) ◽  
pp. 1753-1759 ◽  
Author(s):  
Hirosuke Tatsumi ◽  
Kazuyoshi Takagi ◽  
Megumi Fujita ◽  
Kenji Kano ◽  
Tokuji Ikeda
Keyword(s):  
Methyl Viologen ◽  
Electrochemical Study ◽  
Electron Carrier ◽  
Reversible Hydrogenase

Photoinduced hydrogen evolution with lysine-linked viologen and hydrogenase

2002 ◽  
Vol 06 (01) ◽  
pp. 26-32 ◽  
Author(s):  
Noriyuki Asakura ◽  
Akimitsu Miyaji ◽  
Toshiaki Kamachi ◽  
Ichiro Okura
Keyword(s):  
Hydrogen Evolution ◽  
Electron Donor ◽  
Methyl Viologen ◽  
Evolution System ◽  
Electron Carrier ◽  
Effective Hydrogen

Lysine-linked viologen was prepared as a substrate for the hydrogenase. By using reduced lysine-linked viologen ( LysV +•), the hydrogenase- LysV +• complex was formed efficiently, leading to effective hydrogen evolution compared with methyl viologen. Lysine-linked viologen as an electron carrier was applied for the photoinduced hydrogen evolution system containing hydrogenase, Tetrakis(4-carboxyphenyl)porphyrin ( TCPP ) as a photosensitizer, and a sacrificial electron donor for TCPP . In this system, effective photoinduced hydrogen evolution was observed.

scholarly journals Development of a proteoliposome model to probe transmembrane electron-transfer reactions

2012 ◽  
Vol 40 (6) ◽  
pp. 1257-1260 ◽  
Author(s):  
Gaye F. White ◽  
Zhi Shi ◽  
Liang Shi ◽  
Alice C. Dohnalkova ◽  
James K. Fredrickson ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Outer Membrane ◽  
Protein Complex ◽  
Methyl Viologen ◽  
Cation Exchanger ◽  
Shewanella Oneidensis ◽  
Model System ◽  
Electron Acceptors ◽  
Transfer Reactions ◽  
Electron Carrier

The mineral-respiring bacterium Shewanella oneidensis uses a protein complex, MtrCAB, composed of two decahaem cytochromes brought together inside a transmembrane porin to transport electrons across the outer membrane to a variety of mineral-based electron acceptors. A proteoliposome system has been developed that contains Methyl Viologen as an internalized electron carrier and valinomycin as a membrane-associated cation exchanger. These proteoliposomes can be used as a model system to investigate MtrCAB function.

scholarly journals Purification of the membrane-bound hydrogenase of Escherichia coli

1979 ◽  
Vol 183 (1) ◽  
pp. 11-22 ◽  
Author(s):  
M W W Adams ◽  
D O Hall
Keyword(s):  
Escherichia Coli ◽  
Methyl Viologen ◽  
Hydrophobic Interaction Chromatography ◽  
H2 Evolution ◽  
Ph Optimum ◽  
Benzyl Viologen ◽  
Electron Carrier ◽  
Membrane Bound ◽  
High Concentrations ◽  
Electron Carriers

The membrane-bound hydrogenase (EC class 1.12) of aerobically grown Escherichia coli cells was solubilized by treatment with deoxycholate and pancreatin. The enzyme was further purified to electrophoretic homogeneity by chromoatographic methods, including hydrophobic-interaction chromatography, with a yield of 10% as judged by activity and an overall purification of 2140-fold. The hydrogenase was a dimer of identical subunits with a mol.wt. of 113,000 and contained 12 iron and 12 acid-labile sulphur atoms per molecule. The epsilon 400 was 49,000M-1 . cm-1. The hydrogenase catalysed both H2 evolution and H2 uptake with a variety of artificial electron carriers, but would not interact with flavodoxin, ferredoxin or nicotinamide and flavin nucleotides. We were unable to identify any physiological electron carrier for the hydrogenase. With Methyl Viologen as the electron carrier, the pH optimum for H2 evolution and H2 uptake was 6.5 and 8.5 respectively. The enzyme was stable for long periods at neutral pH, low temperatures and under anaerobic conditions. The half-life of the hydrogenase under air at room temperature was about 12 h, but it could be stabilized by Methyl Viologen and Benzyl Viologen, both of which are electron carriers for the enzyme, and by bovine serum albumin. The hydrogenase was strongly inhibited by carbon monoxide (Ki = 1870Pa), heavy-metal salts and high concentrations of buffers, but was resistant to inhibition by thiol-blocking and metal-complexing reagents. These aerobically grown E. coli cells lacked formate hydrogenlyase activity and cytochrome c552.

Impact of the donor substituent on the optoelectrochemical properties of 6H-indolo[2,3-b]quinoxaline amine derivatives

2019 ◽  
Vol 43 (48) ◽  
pp. 19379-19396 ◽  
Author(s):  
Pooja S. Singh ◽  
Purav M. Badani ◽  
Rajesh M. Kamble
Keyword(s):  
Electrochemical Study ◽  
Donor Substituent

An opto-electrochemical study of D–A based indolo-quinoxaline amine derivatives was performed by varying the strength of the amine substituent.

Electrochemical Study of DNA Damaged by Oxidation Stress

2013 ◽  
Vol 16 (2) ◽  
pp. 130-141
Author(s):  
Ondrej Zitka ◽  
Sona Krizkova ◽  
Sylvie Skalickova ◽  
Pavel Kopel ◽  
Petr Babula ◽  
...  
Keyword(s):  
Electrochemical Study ◽  
Oxidation Stress
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