Electrostatic interactions in globular proteins: calculation of the pH dependence of the redox potential of cytochrome c551.
An equal mixture of oxidized and reduced cytochrome c551 experiences a change in the potential of the haem iron when one of the propionates attached to the haem is ionized. The change is 65 mV, which corresponds to an effective dielectric between the propionate and the iron of 27. It has been possible to use the algorithm of Warwicker & Watson (1982) to calculate the change in the potential at the haem iron arising from the change in ionization of the propionate. This gives the extra work required to oxidize or reduce the iron. The change in potential that we calculate is 90 mV, which corresponds to an effective dielectric of 19.5, between the propionate and the iron. In comparison with other commonly used dielectric models the agreement is very good.
Rogers
N K
NK
Moore
G R
GR
Sternberg
M J
MJ
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D004560:Electricity; D006418:Heme; D006863:Hydrogen-Ion Concentration; D007501:Iron; D008954:Models, Biological; D010084:Oxidation-Reduction; D011422:Propionates
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D011422:Propionates; D006418:Heme; C017167:cytochrome C(551); D007501:Iron; C029658:propionic acid