Article
Mutation of the heme axial ligand of Escherichia coli succinate-quinone reductase: implications for heme ligation in mitochondrial complex II from yeast.
Biochimica et biophysica acta - 1 Jan 2000
Maklashina Elena, Rajagukguk Sany, McIntire William S, Cecchini Gary
Abstract excerpt
A b-type heme is conserved in membrane-bound complex II enzymes (SQR, succinate-ubiquinone reductase). The axial ligands for the low spin heme b in Escherichia coli complex II are SdhC His84 and SdhD His71. E. coli SdhD His71 is separated by 10 residues from SdhD Asp82 and Tyr83 which are essential for ubiquinone catalysis. The same His-10x-AspTyr motif dominates in homologous SdhD proteins, except for...
Topics
- Amino Acid Motifs
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Base Sequence
- Cattle
- DNA Primers
- Electron Transport Complex II
- Escherichia coli
- Escherichia coli Proteins