The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.

The properties of a cpYFP [circularly permuted YFP (yellow fluorescent protein)] reported to act as a superoxide sensor have been re-examined in Arabidopsis mitochondria. We have found that the probe has high pH sensitivity and that dynamics in the cpYFP signal disappeared when the matrix pH was cla...

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Main Authors: Schwarzländer, M, Logan, D, Fricker, M, Sweetlove, L
Format: Journal article
Language:English
Published: 2011
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author Schwarzländer, M
Logan, D
Fricker, M
Sweetlove, L
author_facet Schwarzländer, M
Logan, D
Fricker, M
Sweetlove, L
author_sort Schwarzländer, M
collection OXFORD
description The properties of a cpYFP [circularly permuted YFP (yellow fluorescent protein)] reported to act as a superoxide sensor have been re-examined in Arabidopsis mitochondria. We have found that the probe has high pH sensitivity and that dynamics in the cpYFP signal disappeared when the matrix pH was clamped by nigericin. In contrast, genetic and pharmacological manipulation of matrix superoxide had no detectable effect on the cpYFP signal. These findings question the existence of superoxide flashes in mitochondria.
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spelling oxford-uuid:874d54ab-59d1-4352-aa7f-06a015a363712022-03-26T22:09:49ZThe circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:874d54ab-59d1-4352-aa7f-06a015a36371EnglishSymplectic Elements at Oxford2011Schwarzländer, MLogan, DFricker, MSweetlove, LThe properties of a cpYFP [circularly permuted YFP (yellow fluorescent protein)] reported to act as a superoxide sensor have been re-examined in Arabidopsis mitochondria. We have found that the probe has high pH sensitivity and that dynamics in the cpYFP signal disappeared when the matrix pH was clamped by nigericin. In contrast, genetic and pharmacological manipulation of matrix superoxide had no detectable effect on the cpYFP signal. These findings question the existence of superoxide flashes in mitochondria.
spellingShingle Schwarzländer, M
Logan, D
Fricker, M
Sweetlove, L
The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.
title The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.
title_full The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.
title_fullStr The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.
title_full_unstemmed The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.
title_short The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'.
title_sort circularly permuted yellow fluorescent protein cpyfp that has been used as a superoxide probe is highly responsive to ph but not superoxide in mitochondria implications for the existence of superoxide flashes
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