The role of electrostatics in proton‐conducting membrane protein complexes

FEBS Letters

Lancaster, C.Roy D.¹ 

[1] Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, Marie-Curie-Str. 15, D-60439 Frankfurt am Main, Germany

关键词: Cytochrome c oxidase;    Electron transfer;    Photosynthetic reaction center;    Proton transfer;    Quinol:fumarate reductase;    COX;    cytochrome c oxidase;    H+ i;    a proton from the ‘inner’ (cytoplasmic or matrix) phase;    H+ o;    a proton from the ‘outer’ (periplasmic or intermembrane) phase;    QFR;    quinol:fumarate reductase;    RC;    photosynthetic reaction center;    SQORs;    succinate:quinone-oxidoreductases;    SQR;    succinate:quinone reductase;    ΔG crg(i;    j);    pairwise interaction energy of ionizable residue i with other ionizable residues j;    ΔG pol;    interaction energy with the protein backbone and polar side chains;    ΔG rxn;    reaction field energy;    μ;    dipole length;    θ;    angle of the dipole axis relative to the position of interest;   

DOI  :  10.1016/S0014-5793(03)00393-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Electrostatic interactions play a key role in the coupling of electron and proton transfer in membrane protein complexes during the conversion of the energy stored in sunlight or reduced substrates into biochemical energy via a transmembrane electrochemical proton potential. Principles of charge stabilization within membrane proteins are reviewed and discussed for photosynthetic reaction centers, cytochrome c oxidases, and diheme-containing quinol:fumarate reductases. The impact of X-ray structure-based electrostatic calculations on the functional interpretation of these structural coordinates, on providing new explanations for experimental observations, and for the design of more focused additional experiments is illustrated by a number of key examples.

【 授权许可】

Unknown