Modulation of redox potential in electron transfer proteins: Effects of complex formation on the active site microenvironment of cytochrome b5

2000 ◽  
Vol 116 ◽  
pp. 221-234 ◽  
Author(s):  
Marc Wirtz ◽  
Vaheh Oganesyan ◽  
Xuejun Zhang ◽  
Joe Studer ◽  
Mario Rivera
1973 ◽  
Vol 133 (2) ◽  
pp. 283-287 ◽  
Author(s):  
R. J. Kassner ◽  
W. Yang

The two-iron–sulphur co-ordination centre in plant and algal ferredoxins is considered as a collection of charged ions whose net negative charge is twice that of the one-iron–sulphur protein rubredoxin. Calculation of the electrostatic free-energy changes for reduction of the two types of proteins indicates that the redox potential of the two-iron–sulphur proteins should be more negative than that of the one-iron–sulphur protein and that in biological systems the ferredoxins should function as one-electron transfer proteins.


2012 ◽  
Vol 40 (2) ◽  
pp. 415-418 ◽  
Author(s):  
Marcellus Ubbink

Recent studies have provided experimental information about the initial stage of protein complex formation, the encounter complex. This stage is particularly important in the weak and transient complexes formed between electron transfer proteins and their partners. These studies are discussed and the role of the encounter complex is interpreted in terms of the specific requirements that the biological function puts on these complexes.


1987 ◽  
Vol 52 (7) ◽  
pp. 1658-1665
Author(s):  
Viktor Řehák ◽  
Jana Boledovičová

Disodium 1,5- and 1,8-anthracenedisulphonate (ADS) and 9-acetylanthracene form coloured CT complexes with methylviologen (MV2+) in aqueous and micellar media. The complex formation constants and molar absorptivities were determined by the Benesi-Hildebrandt method. In the fluorescence quenching, its static component plays the major role. The dynamic quenching component is determined by the rate constant of electron transfer from the S1 state of ADS to MV2+.


Sign in / Sign up

Export Citation Format

Share Document