From model compounds to protein binding: syntheses, characterizations and fluorescence studies of [RuII(bipy)(terpy)L]2+complexes (bipy = 2,2′-bipyridine; terpy = 2,2′:6′,2″-terpyridine; L = imidazole, pyrazole and derivatives, cytochrome c)

2005 ◽  
pp. 256-267 ◽  
Author(s):  
Xiao-Juan Yang ◽  
Friedrich Drepper ◽  
Biao Wu ◽  
Wen-Hua Sun ◽  
Wolfgang Haehnel ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Protein Binding ◽  
Model Compounds ◽  
Fluorescence Studies

Stopped-Flow Fluorescence Studies of HMG-Domain Protein Binding to Cisplatin-Modified DNA†

Biochemistry ◽  
2000 ◽  
Vol 39 (29) ◽  
pp. 8426-8438 ◽  
Author(s):  
Elizabeth R. Jamieson ◽  
Stephen J. Lippard
Keyword(s):  
Protein Binding ◽  
Stopped Flow ◽  
Fluorescence Studies ◽  
Modified Dna ◽  
Domain Protein

Activation of Platinum(IV) Prodrugs by Cytochrome c and Characterization of the Protein Binding Sites

2016 ◽  
Vol 13 (9) ◽  
pp. 3216-3223 ◽  
Author(s):  
Alessia Lasorsa ◽  
Olga Stuchlíková ◽  
Viktor Brabec ◽  
Giovanni Natile ◽  
Fabio Arnesano
Keyword(s):  
Cytochrome C ◽  
Protein Binding ◽  
Binding Sites ◽  
Protein Binding Sites

Effects of Specific Anion-Protein Binding on the Alkaline Transition of Cytochrome c

2001 ◽  
Vol 386 (1) ◽  
pp. 117-122 ◽  
Author(s):  
Gianantonio Battistuzzi ◽  
Marco Borsari ◽  
Antonio Ranieri ◽  
Marco Sola
Keyword(s):  
Cytochrome C ◽  
Protein Binding ◽  
Alkaline Transition

Spectroscopic and electrochemical studies of novel model compounds for cytochrome c oxidase

2010 ◽  
Vol 363 (10) ◽  
pp. 2201-2208 ◽  
Author(s):  
Kalliopi Ladomenou ◽  
Georgios Charalambidis ◽  
Athanassios G. Coutsolelos
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Electrochemical Studies ◽  
Model Compounds ◽  
Novel Model

scholarly journals The role of succinate in the respiratory chain of Trypanosoma brucei procyclic trypomastigotes

1989 ◽  
Vol 259 (2) ◽  
pp. 363-368 ◽  
Author(s):  
J F Turrens
Keyword(s):  
Cytochrome C ◽  
Trypanosoma Brucei ◽  
Respiratory Chain ◽  
Intact Cell ◽  
Inhibitory Effect ◽  
Fumarate Reductase ◽  
Glycerol Phosphate ◽  
Intact Cells ◽  
Fluorescence Studies ◽  
Nadh Cytochrome

Trypanosoma brucei procyclic trypomastigotes were made permeable by using digitonin (0-70 micrograms/mg of protein). This procedure allowed exposure of coupled mitochondria to different substrates. Only succinate and glycerol phosphate (but not NADH-dependent substrates) were capable of stimulating oxygen consumption. Fluorescence studies on intact cells indicated that addition of succinate stimulates NAD(P)H oxidation, contrary to what happens in mammalian mitochondria. Addition of malonate, an inhibitor of succinate dehydrogenase, stimulated NAD(P)H reduction. Malonate also inhibited intact-cell respiration and motility, both of which were restored by further addition of succinate. Experiments carried out with isolated mitochondrial membranes showed that, although the electron transfer from succinate to cytochrome c was inhibitable by antimycin, NADH-cytochrome c reductase was antimycin-insensitive. We postulate that the NADH-ubiquinone segment of the respiratory chain is replaced by NADH-fumarate reductase, which reoxidizes the mitochondrial NADH and in turn generates succinate for the respiratory chain. This hypothesis is further supported by the inhibitory effect on cell growth and respiration of 3-methoxyphenylacetic acid, an inhibitor of the NADH-fumarate reductase of T. brucei.

Electrocatalytic four-electron reductions of O2 to H2O with cytochrome c oxidase model compounds

2003 ◽  
Vol 48 (27) ◽  
pp. 4077-4082 ◽  
Author(s):  
Hyosul Shin ◽  
Dong-Heon Lee ◽  
Chan Kang ◽  
Kenneth D. Karlin
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Model Compounds

Effect of different drugs on a cytochrome c – phospholipid bilayer membrane

1978 ◽  
Vol 56 (4) ◽  
pp. 555-563
Author(s):  
Michael A. Singer
Keyword(s):  
Cytochrome C ◽  
Protein Binding ◽  
Lipid Vesicles ◽  
Bilayer Membrane ◽  
Fatty Acyl ◽  
Phospholipid Bilayer ◽  
Butylated Hydroxytoluene ◽  
Na Permeability ◽  
Na Efflux ◽  
Temperature Interaction

Liposomes were prepared from dipalmitoyl phosphatidylcholine and dicetylphosphate and their interaction with the extrinsic membrane protein cytochrome c examined in terms of changes in 22Na permeability, electrophoretic mobility, protein binding, and motion of an incorporated spin label. The amount of cytochrome c bound displays no significant temperature dependence over the temperature range studied (from 30 to 55 °C) whereas cytochrome c causes an increase in 22Na efflux only above the phospholipid phase transition temperature. Interaction of the protein with the lipid vesicles causes no significant disturbance in the bilayer interior as monitored by the motion of the incorporated spin probe. The drugs 2,4-dinitrophenol and ethacrynic acid, both of which increase the magnitude of the vesicle negative charge, enhance both cytochrome c binding and its effect on 22Na permeability. In contrast, the local anesthetic dibucaine, which induces a positive surface charge on these liposomes, reduces both protein binding and the protein-induced increase in 22Na efflux. Finally, the chemicals butylated hydroxytoluene, 2-tert-butylphenol, and tert-butylbenzene, all of which cause early 'melting' of the phospholipid fatty acyl chains, block the capacity of cytochrome c to enhance 22Na permeability while having no effect on its binding to the vesicles.

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