Characterizing the effects of the protein environment on the reduction potentials of metalloproteins.

ABSTRACT: The reduction potentials of electron transfer proteins are critically determined by the degree of burial of the redox site within the protein and the degree of permanent polarization of the polypeptide around the redox site. Although continuum electrostatics calculations of protein structures can predict the net effect of these factors, quantifying each individual contribution is a difficult task. Here, the burial of the redox site is characterized by a dielectric radius R(p) (a Born-type radius for the protein), the polarization of the polypeptide is characterized by an electret potential ϕ(p) (the average electrostatic potential at the metal atoms), and an electret-dielectric spheres (EDS) model of the entire protein is then defined in terms of R(p) and ϕ(p). The EDS model shows that for

SUBMITTER: Perrin BS 

PROVIDER: S-EPMC3567609 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature