Compelling EPR evidence that the alternative oxidase is a diiron carboxylate protein

Anthony L. Moore; Jane E. Carré; Charles Affourtit; Mary S. Albury; Paul G. Crichton; Kiyoshi Kita; Peter Heathcote

doi:10.1016/j.bbabio.2008.01.004

Compelling EPR evidence that the alternative oxidase is a diiron carboxylate protein

Anthony L. Moore, Jane E. Carré, Charles Affourtit, Mary S. Albury, Paul G. Crichton, Kiyoshi Kita, Peter Heathcote

Research output: Contribution to journal › Article › peer-review

49 Citations (Scopus)

Abstract

The alternative oxidase is a respiratory chain protein found in plants, fungi and some parasites that still remains physically uncharacterised. In this report we present EPR evidence from parallel mode experiments which reveal signals at approximately g = 16 in both purified alternative oxidase protein (g = 16.9), isolated mitochondrial membranes (g = 16.1), and in trypanosomal AOX expressed in Escherichia coli membranes (g = 16.4). Such signals are indicative of a dicarboxylate diiron centre at the active site of the enzyme. To our knowledge these data represent the first EPR signals from AOX present in its native environment.

Original language	English
Pages (from-to)	327-330
Number of pages	4
Journal	Biochimica Et Biophysica Acta-Bioenergetics
Volume	1777
Issue number	4
Early online date	17 Jan 2008
DOIs	https://doi.org/10.1016/j.bbabio.2008.01.004
Publication status	Published - Apr 2008
Externally published	Yes

Keywords

Alternative oxidase
Diiron
Electron transfer
Monotopic integral membrane protein
Respiration

Access to Document

10.1016/j.bbabio.2008.01.004Licence: Other

Cite this

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title = "Compelling EPR evidence that the alternative oxidase is a diiron carboxylate protein",

abstract = "The alternative oxidase is a respiratory chain protein found in plants, fungi and some parasites that still remains physically uncharacterised. In this report we present EPR evidence from parallel mode experiments which reveal signals at approximately g = 16 in both purified alternative oxidase protein (g = 16.9), isolated mitochondrial membranes (g = 16.1), and in trypanosomal AOX expressed in Escherichia coli membranes (g = 16.4). Such signals are indicative of a dicarboxylate diiron centre at the active site of the enzyme. To our knowledge these data represent the first EPR signals from AOX present in its native environment.",

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T1 - Compelling EPR evidence that the alternative oxidase is a diiron carboxylate protein

AU - Moore, Anthony L.

AU - Carré, Jane E.

AU - Affourtit, Charles

AU - Albury, Mary S.

AU - Crichton, Paul G.

AU - Kita, Kiyoshi

AU - Heathcote, Peter

PY - 2008/4

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AB - The alternative oxidase is a respiratory chain protein found in plants, fungi and some parasites that still remains physically uncharacterised. In this report we present EPR evidence from parallel mode experiments which reveal signals at approximately g = 16 in both purified alternative oxidase protein (g = 16.9), isolated mitochondrial membranes (g = 16.1), and in trypanosomal AOX expressed in Escherichia coli membranes (g = 16.4). Such signals are indicative of a dicarboxylate diiron centre at the active site of the enzyme. To our knowledge these data represent the first EPR signals from AOX present in its native environment.

KW - Alternative oxidase

KW - Diiron

KW - Electron transfer

KW - Monotopic integral membrane protein

KW - Respiration

U2 - 10.1016/j.bbabio.2008.01.004

DO - 10.1016/j.bbabio.2008.01.004

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AN - SCOPUS:40949110571

VL - 1777

SP - 327

EP - 330

JO - Biochimica Et Biophysica Acta-Bioenergetics

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