| Literature DB >> 12633849 |
Coichi Nihei1, Yoshihisa Fukai, Keisuke Kawai, Arihiro Osanai, Yoshisada Yabu, Takashi Suzuki, Nobuo Ohta, Nobuko Minagawa, Kazuo Nagai, Kiyoshi Kita.
Abstract
Trypanosome alternative oxidase (TAO) is the terminal oxidase of the respiratory chain in long slender bloodstream forms of African trypanosomes. TAO is a cytochrome-independent, cyanide-insensitive quinol oxidase. These characteristics are distinct from those of the bacterial quinol oxidases, proteins that belong to the heme-copper terminal oxidase superfamily. The inability to purify stable TAO has severely hampered biochemical studies of the alternative oxidase family. In the present study, we were able to purify recombinant TAO to homogeneity from Escherichia coli membranes using the detergent digitonin. Kinetic analysis of the purified TAO revealed that the specific inhibitor ascofuranone is a competitive inhibitor of ubiquinol oxidase activity.Entities:
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Year: 2003 PMID: 12633849 DOI: 10.1016/s0014-5793(03)00120-0
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124