The photochemistry of Ru(bpy)32+ in basic medium

Ru(bpy)32+ is photodecomposed in 0.3 M NaOH with [Formula: see text]. With methyl viologen also present, electron transfer quenching of the luminescence is accompanied by formation of the one electron reduction product of methyl viologen, MV+. The Ru(bpy)33+ formed in the corresponding oxidation is rapidly reduced by either OH− or MV+ to Ru(II).

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Interfacial interactions and the heterogeneous one-electron reduction of methyl viologen

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19871097 ◽

1987 ◽

Vol 52 (5) ◽

pp. 1097-1114 ◽

Cited By ~ 14

Author(s):

Michael Heyrovský ◽

Ladislav Novotný

Keyword(s):

Electron Transfer ◽

Radical Cation ◽

Electrode Surface ◽

Methyl Viologen ◽

Potential Range ◽

Standard Redox Potential ◽

Mercury Electrodes ◽

Electron Reduction ◽

The One ◽

Surface Redox

The one-electron reversible electroreduction of methyl viologen to its radical cation in aqueous solutions on mercury electrodes proceeds, according to potential, concentration and time of electrolysis, in various ways. Methyl viologen is adsorbed in flat orientation at the electrode surface; it undergoes a surface redox process in π-interaction with the metal in a potential range positive by about 0.2 V of the beginning of the electroreduction. The actual reduction starts by electron transfer followed by adsorption of the radical cation and, at higher concentrations and in a narrow potential range, by crystallization at the electrode surface of a salt of the radical cation. In solution near the electrode the radical cation dimerizes and the dimer also adsorbs at the electrode. In the region of the standard redox potential and more negative the reduction proceeds by electron transfer from the electrode covered by a layer of the radical cation or of its dimer.

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On Inhibition of Polarographic Reduction of the Dioxalatocuprate(II) Ion by the One-Electron Reduction Product of Phenylmercury Hydroxide

Bulletin of the Chemical Society of Japan ◽

10.1246/bcsj.45.2233 ◽

1972 ◽

Vol 45 (7) ◽

pp. 2233-2234 ◽

Cited By ~ 2

Author(s):

Teisuke Murayama ◽

Akio Takayanagi

Keyword(s):

Reduction Product ◽

Polarographic Reduction ◽

Electron Reduction ◽

The One

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Identification of two reduction products of glyoxal bis(2-mercaptoanil)nickel. Characterization of the one-electron reduction product and the partially hydrogenated anion

Journal of the American Chemical Society ◽

10.1021/ja00986a008 ◽

1967 ◽

Vol 89 (10) ◽

pp. 2278-2281 ◽

Cited By ~ 19

Author(s):

F. Lalor ◽

M. Frederick. Hawthorne ◽

August H. Maki ◽

K. Darlington ◽

Alan. Davison ◽

...

Keyword(s):

Reduction Product ◽

Electron Reduction ◽

The One

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Theoretical insights into the reductive metabolism of CCl4 by cytochrome P450 enzymes and the CCl4-dependent suicidal inactivation of P450

Dalton Transactions ◽

10.1039/c4dt02065k ◽

2014 ◽

Vol 43 (39) ◽

pp. 14833-14840 ◽

Cited By ~ 12

Author(s):

Xiao-Xi Li ◽

Qing-Chuan Zheng ◽

Yong Wang ◽

Hong-Xing Zhang

Keyword(s):

Cytochrome P450 ◽

Reduction Product ◽

Cytochrome P450 Enzymes ◽

Electron Reduction ◽

The One ◽

Reductive Metabolism

The one-electron reduction product, ˙CCl3, irreversibly inactivates P450 via covalently binding to the meso-carbon, whereas the two successive one-electron reductions product, :CCl2, reversibly inhibits P450 by coordinating to iron.

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Reduction of ferric haemoproteins by tetrahydropterins: a kinetic study

Biochemical Journal ◽

10.1042/bj20050437 ◽

2005 ◽

Vol 392 (3) ◽

pp. 583-587 ◽

Cited By ~ 10

Author(s):

Chantal Capeillere-Blandin ◽

Delphine Mathieu ◽

Daniel Mansuy

Keyword(s):

Electron Transfer ◽

Cytochrome C ◽

Cytochrome B5 ◽

Reduction Rate ◽

Cation Radical ◽

Order Reduction ◽

Reduction Potentials ◽

Electron Reduction ◽

The One

We previously showed that one-electron transfer from tetrahydropterins to iron porphyrins is a very general reaction, with formation of an intermediate cation radical similar to the one detected in NO synthase. As a model reaction, the rates of reduction of eight haemoproteins by diMePH4 (6,7-dimethyltetrahydropterin) have been studied and correlated with their one-electron reduction potentials, Em (FeIII/FeII). On the basis of kinetic data analyses, a bimolecular collisional mechanism is proposed for the electron transfer from diMePH4 to ferrihaemoproteins. Haemoproteins with reduction potentials below −160 mV were shown not to be reduced by diMePH4 to the corresponding ferrohaemoproteins. For haemoproteins with reduction potentials more positive than −160 mV, such as chloroperoxidase, cytochrome b5, methaemoglobin and cytochrome c, there was a good correlation between the second-order reduction rate constant and the redox potential, Em (FeIII/FeII):The rate of reduction of cytochrome c by BH4 [(6R)-5,6,7,8-tetrahydrobiopterin] was determined to be similar to that of the reduction of cytochrome c by diMePH4. These results confirm the role of tetrahydropterins as one-electron donors to FeIII porphyrins.

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