Difference between revisions of "Young 2013 Biochem Soc Trans"
(Created page with "{{Publication |title=Young L, Shiba T, Harada S, Kita K, Albury MS, Moore AL (2013) The alternative oxidases: simple oxidoreductase proteins with complex functions. Biochem So...") |
|||
| Line 2: | Line 2: | ||
|title=Young L, Shiba T, Harada S, Kita K, Albury MS, Moore AL (2013) The alternative oxidases: simple oxidoreductase proteins with complex functions. Biochem Soc Trans 41:1305-11. | |title=Young L, Shiba T, Harada S, Kita K, Albury MS, Moore AL (2013) The alternative oxidases: simple oxidoreductase proteins with complex functions. Biochem Soc Trans 41:1305-11. | ||
|info=[https://www.ncbi.nlm.nih.gov/pubmed/24059524 PMID: 24059524] | |info=[https://www.ncbi.nlm.nih.gov/pubmed/24059524 PMID: 24059524] | ||
|authors=Young L, Shiba T, Harada S, Kita K, Albury MS, Moore | |authors=Young L, Shiba T, Harada S, Kita K, Albury MS, Moore Anthoy L | ||
|year=2013 | |year=2013 | ||
|journal=Biochem Soc Trans | |journal=Biochem Soc Trans | ||
| Line 12: | Line 12: | ||
|area=Respiration | |area=Respiration | ||
|preparations=Enzyme, Oxidase;biochemical oxidation | |preparations=Enzyme, Oxidase;biochemical oxidation | ||
|additional=AOX, | |||
}} | }} | ||
Revision as of 12:09, 7 March 2020
| Young L, Shiba T, Harada S, Kita K, Albury MS, Moore AL (2013) The alternative oxidases: simple oxidoreductase proteins with complex functions. Biochem Soc Trans 41:1305-11. |
Young L, Shiba T, Harada S, Kita K, Albury MS, Moore Anthoy L (2013) Biochem Soc Trans
Abstract: The alternative oxidases are membrane-bound monotopic terminal electron transport proteins found in all plants and in some agrochemically important fungi and parasites including Trypansoma brucei, which is the causative agent of trypanosomiasis. They are integral membrane proteins and reduce oxygen to water in a four electron process. The recent elucidation of the crystal structure of the trypanosomal alternative oxidase at 2.85 Å (1 Å=0.1 nm) has revealed salient structural features necessary for its function. In the present review we compare the primary and secondary ligation spheres of the alternative oxidases with other di-iron carboxylate proteins and propose a mechanism for the reduction of oxygen to water. • Keywords: AOX • Bioblast editor: Gnaiger E
Labels: MiParea: Respiration
Preparation: Enzyme, Oxidase;biochemical oxidation
AOX
