Rieske iron-sulfur proteins from extremophilic organisms.
Proteins located on the outside of the membranes of organisms thriving under extreme conditions like high or low pH, or high salinity face special challenges maintaining their structural integrity. This review is focused on the Rieske iron-sulfur proteins from these organisms. Rieske proteins are essential subunits of the cytochrome bc-complexes, which are often of crucial importance for the energy metabolism of the cells. On the basis of the available data we propose strategies by which these proteins are able to stabilize their noncovalent bound cofactor and adapt to the function under extreme conditions.
Schmidt
C L
CL
Institut für Biochemie der Universität Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany. schmidt@biochem.uni-luebeck.de
D000222:Adaptation, Physiological / Q000502:physiology; D001105:Archaea / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D014450:Electron Transport Complex III / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D055672:Static Electricity; D013329:Structure-Activity Relationship; D013696:Temperature
D019843:Archaeal Proteins; D007506:Iron-Sulfur Proteins; C037989:Rieske iron-sulfur protein; D014450:Electron Transport Complex III