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The alternative oxidases: simple oxidoreductase proteins with complex functions
Luke Young1, Tomoo Shiba, Shigeharu Harada
1*Department of Biochemistry and Molecular Biology, School of Life Sciences, University of Sussex, Brighton BN1 9QG, U.K.
Alternative oxidases, crucial electron transport proteins in plants and parasites like Trypanosoma brucei, reduce oxygen to water. Their structure and function are compared to other di-iron proteins, proposing a novel oxygen reduction mechanism.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Alternative oxidases are essential membrane-bound proteins in plants, fungi, and parasites.
- These proteins play a vital role in cellular respiration by reducing oxygen to water.
- Trypanosoma brucei, a parasite causing trypanosomiasis, possesses a significant alternative oxidase.
Purpose of the Study:
- To compare the ligation spheres of alternative oxidases with other di-iron carboxylate proteins.
- To elucidate the structural features of the trypanosomal alternative oxidase.
- To propose a mechanism for oxygen reduction by alternative oxidases.
Main Methods:
- Structural analysis of the trypanosomal alternative oxidase at 2.85 Å resolution.
- Comparative analysis of primary and secondary ligation spheres.
- Bioinformatic and biochemical comparisons with related di-iron proteins.
Main Results:
- The crystal structure revealed key functional features of the trypanosomal alternative oxidase.
- Significant similarities and differences were identified in the ligation spheres.
- A proposed mechanism for the four-electron reduction of oxygen to water was developed.
Conclusions:
- Alternative oxidases share conserved structural motifs with other di-iron carboxylate proteins.
- Structural insights facilitate understanding of the oxygen reduction mechanism.
- This review provides a framework for further investigation into alternative oxidase function and inhibition.
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