title: Inside view of a giant proton pump.
abstract: Inner workings: The X-ray crystal structure of the entire bacterial complex I at 3.3 Å resolution offers fascinating insights into a giant 536 kDa molecular machine. The respiratory chain complex seems to employ unique mechanisms of energetic coupling that are entirely different from those found in all other enzymes using redox energy to drive vectorial proton transport across a bioenergetic membrane.
authors.affiliation: Exzellenzcluster Macromolecular Complexes, Goethe-Universität, Frankfurt am Main, Germany. u.brandt@cukz.umcn.nl
authors.forename: Ulrich
authors.initials: U
authors.lastname: Brandt
mesh_terms: D001692:Biological Transport; D018360:Crystallography, X-Ray; D042967:Electron Transport Complex I / Q000737:chemistry* / Q000378:metabolism; D005486:Flavin Mononucleotide / Q000737:chemistry / Q000378:metabolism; D010085:Oxidative Phosphorylation; D020836:Protein Structure, Quaternary; D011522:Protons; D016963:Thermus thermophilus / Q000378:metabolism*
chemical_list: D011522:Protons; D005486:Flavin Mononucleotide; D042967:Electron Transport Complex I
keywords: bioenergetics; complex I; proton pumps; structure elucidation; ubiquinone