Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins.
Klingen
Astrid R
AR
Department of Structural Biology/Bioinformatics, Bayreuth University, Universitätsstrasse 30, BGI, D-95447 Bayreuth, Germany.
Ullmann
G Matthias
GM
D000818:Animals; D001224:Aspartic Acid / Q000235:genetics; D019117:Burkholderia / Q000201:enzymology; D002417:Cattle; D003198:Computer Simulation; D014450:Electron Transport Complex III / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005288:Ferredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018698:Glutamic Acid / Q000235:genetics; D005973:Glutamine / Q000235:genetics; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008024:Ligands; D008956:Models, Chemical; D016297:Mutagenesis, Site-Directed; D012242:Rhodobacter sphaeroides / Q000201:enzymology; D055672:Static Electricity; D013816:Thermodynamics; D017186:Titrimetry
D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D008024:Ligands; C037989:Rieske iron-sulfur protein; D005973:Glutamine; D001224:Aspartic Acid; D018698:Glutamic Acid; D006639:Histidine; D014450:Electron Transport Complex III