Internal electron transfer in a quinone adduct of a nickel(II)-catecholate complex

1988 ◽  
Vol 110 (20) ◽  
pp. 6897-6898 ◽  
Author(s):  
Cristiano. Benelli ◽  
Andrea. Dei ◽  
Dante. Gatteschi ◽  
Luca. Pardi
Keyword(s):  
Electron Transfer ◽  
Catecholate Complex ◽  
Internal Electron

ChemInform Abstract: Internal Electron Transfer in a Quinone Adduct of a Nickel(II)-Catecholate Complex.

ChemInform ◽  
1989 ◽  
Vol 20 (2) ◽  
Author(s):  
C. BENELLI ◽  
A. DEI ◽  
D. GATTESCHI ◽  
L. PARDI
Keyword(s):  
Electron Transfer ◽  
Catecholate Complex ◽  
Internal Electron

scholarly journals Filling the catalytic site of cytochrome c oxidase with electrons. REDUCED CuB FACILITATES INTERNAL ELECTRON TRANSFER TO HEME a3. VOLUME 281 (2006) PAGES 20003-20010

2006 ◽  
Vol 281 (36) ◽  
pp. 26768
Author(s):  
Daniel Jancura ◽  
Marian Antalik ◽  
Vladimir Berka ◽  
Graham Palmer ◽  
Marian Fabian
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Catalytic Site ◽  
Internal Electron

Accelerated Fe2+ Regeneration in an Effective Electro-Fenton Process by Boosting Internal Electron Transfer to a Nitrogen-Conjugated Fe(III) Complex

2021 ◽  
Author(s):  
Mingyue Liu ◽  
Zhiyuan Feng ◽  
Xinmiao Luan ◽  
Wenhai Chu ◽  
Hongying Zhao ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Fenton Process ◽  
Internal Electron

scholarly journals Internal Electron Transfer between Hemes and Cu(II) Bound at Cysteine β93 Promotes Methemoglobin Reduction by Carbon Monoxide

1999 ◽  
Vol 274 (9) ◽  
pp. 5499-5507 ◽  
Author(s):  
Celia Bonaventura ◽  
Gerald Godette ◽  
Shirley Tesh ◽  
David E. Holm ◽  
Joseph Bonaventura ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Electron Transfer ◽  
Internal Electron

Relaxation Kinetics of Cytochrome P450 Reductase:  Internal Electron Transfer Is Limited by Conformational Change and Regulated by Coenzyme Binding†

Biochemistry ◽  
2002 ◽  
Vol 41 (14) ◽  
pp. 4626-4637 ◽  
Author(s):  
Aldo Gutierrez ◽  
Mark Paine ◽  
C. Roland Wolf ◽  
Nigel S. Scrutton ◽  
Gordon C. K. Roberts
Keyword(s):  
Electron Transfer ◽  
Cytochrome P450 ◽  
Conformational Change ◽  
Cytochrome P450 Reductase ◽  
Relaxation Kinetics ◽  
Coenzyme Binding ◽  
P450 Reductase ◽  
Internal Electron ◽  
Kinetics Of

Magnetic nitrogen-doped sludge-derived biochar catalysts for persulfate activation: Internal electron transfer mechanism

2019 ◽  
Vol 364 ◽  
pp. 146-159 ◽  
Author(s):  
Jiangfang Yu ◽  
Lin Tang ◽  
Ya Pang ◽  
Guangming Zeng ◽  
Jiajia Wang ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Transfer Mechanism ◽  
Electron Transfer Mechanism ◽  
Nitrogen Doped ◽  
Internal Electron ◽  
Persulfate Activation

scholarly journals Some electron-transfer reactions involving carbodi-imide-modified cytochrome c

1987 ◽  
Vol 243 (2) ◽  
pp. 379-384 ◽  
Author(s):  
A J Mathews ◽  
T Brittain
Keyword(s):  
Electron Transfer ◽  
Ionic Strength ◽  
Protein Charge ◽  
Native Proteins ◽  
Wide Range ◽  
Internal Electron ◽  
Modified Proteins ◽  
Time Courses ◽  
Low Ionic Strength ◽  
Kinetics Of

The reaction kinetics of native and carbodi-imide-modified tuna and horse heart cytochromes c with both a strong (dithionite) and a relatively weak (ascorbate) reducing agent were studied over a wide range of conditions. In their reactions with dithionite both the native and modified cytochromes exhibit single exponential time courses. The effects of dithionite concentration and ionic strength on the rate of the reduction are complex and can best be explained in terms of the model proposed by Lambeth & Palmer [(1973) J. Biol. Chem. 248, 6095-6103]. According to this model, at low ionic strength the native proteins are reduced almost exclusively by S2O4(2-) whereas the modified proteins showed reactivity towards both S2O4(2-) and SO2.-. These findings are interpreted in terms of the different charge characteristics of the carbodi-imide-modified proteins relative to the native proteins. The findings that the modified proteins react with ascorbate in a biphasic manner are explained as arising from ascorbate binding to a reducible form of the protein, before electron transfer, with an equilibrium between the ascorbate-reducible form of the protein and a non-reducible form. Estimates were obtained for both the ascorbate equilibrium binding constant and the rate constant for the internal electron transfer for both the native and modified horse and tuna proteins. The effect of pH on the reactions indicates that the active reductant in all cases is ascorbate2-. The studies of ascorbate reactivity yield important information concerning the proposed correlation between ascorbate reducibility and the presence of a 695 nm-absorption band, and the study of dithionite reactivity illustrates the effect of protein charge and solution ionic strength on the relative contributions made by the species SO2.- and S2O4(2-) to the reduction of ferricytochrome c.

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