Site-directed Mutagenesis Reveals the Essentiality of the Conserved Residues in the Putative Diiron Active Site of the Trypanosome Alternative Oxidase

• Published in: The Journal of biological chemistry Vol. 277; no. 10; pp. 8187 - 8193
• Main Authors: Ajayi, Wilfred U., Chaudhuri, Minu, Hill, George C.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 08.03.2002; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Motifs; Animals; Binding Sites; Cell Division; Escherichia coli - metabolism; Genetic Complementation Test; Glutamine - chemistry; Heme - chemistry; Histidine - chemistry; Immunoblotting; Iron - metabolism; Models, Genetic; Mutagenesis, Site-Directed; Mutation; Oxidoreductases - chemistry; Oxidoreductases - genetics; Oxidoreductases - metabolism; Plasmids - metabolism; Protein Binding; Protein Structure, Tertiary; Trypanosoma brucei; Trypanosoma brucei brucei - enzymology; trypanosome alternative oxidase

Trypanosoma brucei possesses a non-cytochrome, salicylhydroxamic acid (SHAM)-sensitive ubiquinol:oxygen oxidoreductase known as trypanosome alternative oxidase (TAO). TAO and similar SHAM-sensitive alternative oxidases (AOXs) contain 2–3 conserved diiron-binding motifs (EXXH). Site-directed mutagene...