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

^*Corresponding author for this work

School of Biomedical Sciences

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

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	0
Journal	Biochim Biophys Acta
Volume	1777
Issue number	4
DOIs	https://doi.org/10.1016/j.bbabio.2008.01.004
Publication status	Published - Apr 2008

Keywords

Animals
Binding Sites
Electron Spin Resonance Spectroscopy
Electron Transport
Iron
Mitochondrial Membranes
Mitochondrial Proteins
Oxidoreductases
Plant Proteins
Trypanosoma

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10.1016/j.bbabio.2008.01.004

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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.",

keywords = "Animals, Binding Sites, Electron Spin Resonance Spectroscopy, Electron Transport, Iron, Mitochondrial Membranes, Mitochondrial Proteins, Oxidoreductases, Plant Proteins, Trypanosoma",

author = "Moore, {Anthony L.} and Carr{\'e}, {Jane E.} and Charles Affourtit and Albury, {Mary S.} and Crichton, {Paul G.} and Kiyoshi Kita and Peter Heathcote",

year = "2008",

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doi = "10.1016/j.bbabio.2008.01.004",

language = "English",

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journal = "Biochim Biophys Acta",

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TY - JOUR

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

Y1 - 2008/4

N2 - 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.

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 - Animals

KW - Binding Sites

KW - Electron Spin Resonance Spectroscopy

KW - Electron Transport

KW - Iron

KW - Mitochondrial Membranes

KW - Mitochondrial Proteins

KW - Oxidoreductases

KW - Plant Proteins

KW - Trypanosoma

U2 - 10.1016/j.bbabio.2008.01.004

DO - 10.1016/j.bbabio.2008.01.004

M3 - Article

SN - 0006-3002

VL - 1777

SP - 327

EP - 330

JO - Biochim Biophys Acta

JF - Biochim Biophys Acta

IS - 4

ER -

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

Abstract

Keywords

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