The role of electrostatics in proton-conducting membrane protein complexes.
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.
Lancaster
C Roy D
CR
Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, Marie-Curie-Str. 15, D-60439 Frankfurt am Main, Germany. roy.lancaster@mpibp-frankfurt.mpg.de
D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism; D017136:Ion Transport; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008962:Models, Theoretical; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry / Q000378:metabolism; D011522:Protons; D055672:Static Electricity
D046911:Macromolecular Substances; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D011522:Protons; D010088:Oxidoreductases; C424907:quinol fumarate reductase; D003576:Electron Transport Complex IV