title: Modeling the effects of mutations on the free energy of the first electron transfer from QA- to QB in photosynthetic reaction centers.
abstract: Numerical calculations of the free energy of the first electron transfer in genetically modified reaction centers from Rhodobacter (Rb.) sphaeroides and Rb. capsulatus were carried out from pH 5 to 11. The multiconformation continuum electrostatics (MCCE) method allows side chain, ligand, and water reorientation to be embedded in the calculations of the Boltzmann distribution of cofactor and amino acid ionization states. The mutation sites whose effects have been modeled are L212 and L213 (the L polypeptide) and two in the M polypeptide, M43(44) and M231(233) in Rb. capsulatus (Rb. sphaeroides). The results of the calculations were compared to the experimental data, and very good agreement was found especially at neutral pH. Each mutation removes or introduces ionizable residues, but the protein maintains a net charge close to that in native RCs through ionization changes in nearby residues. This reduces the effect of mutation and makes the changes in state free energy smaller than would be found in a rigid protein. The state energy of QA-QB and QAQB- states have contributions from interactions among the residues as well as with the quinone which is ionized. For example, removing L213Asp, located in the QB pocket, predominantly changes the free energy of the QA-QB state, where the Asp is ionized in native RCs rather than the QAQB- state, where it is neutral. Side chain, hydroxyl, and water rearrangements due to each of the mutations have also been calculated showing water occupancy changes during the QA- to QB electron transfer.
authors.affiliation: Department of Physics, City College of New York, 138 Street & Convent Avenue, New York, New York 10031, USA.
authors.forename: E
authors.initials: E
authors.lastname: Alexov
authors.forename: J
authors.initials: J
authors.lastname: Miksovska
authors.forename: L
authors.initials: L
authors.lastname: Baciou
authors.forename: M
authors.initials: M
authors.lastname: Schiffer
authors.forename: D K
authors.initials: DK
authors.lastname: Hanson
authors.forename: P
authors.initials: P
authors.lastname: Sebban
authors.forename: M R
authors.initials: MR
authors.lastname: Gunner
mesh_terms: D000409:Alanine / Q000235:genetics; D001120:Arginine / Q000235:genetics; D001216:Asparagine / Q000235:genetics; D001224:Aspartic Acid / Q000235:genetics; D004579:Electron Transport; D004735:Energy Transfer / Q000235:genetics; D018698:Glutamic Acid / Q000235:genetics; D005973:Glutamine / Q000235:genetics; D007930:Leucine / Q000235:genetics; D008956:Models, Chemical; D016297:Mutagenesis, Site-Directed; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000235:genetics*; D011809:Quinones / Q000737:chemistry*; D016354:Rhodobacter capsulatus / Q000235:genetics; D012242:Rhodobacter sphaeroides / Q000235:genetics; D055672:Static Electricity; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D045322:Photosynthetic Reaction Center Complex Proteins; D011809:Quinones; D014867:Water; D005973:Glutamine; D001224:Aspartic Acid; D018698:Glutamic Acid; D001216:Asparagine; D001120:Arginine; D007930:Leucine; D000409:Alanine