EPR Detection of Protein-Derived Radicals in the Reaction of H2O2 with Fe Bound in Mitochondrial F1ATPase

Polizio, Francesca; Lippe, Giovanna; Pancrazio, Francesca Di; Desideri, Alessandro; Mavelli, Irene

doi:10.1006/bbrc.1999.1137

Cited by 6 publications

(3 citation statements)

References 35 publications

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“…In denaturing 1‐D PAGE analysis, however, the decrease in ATPase levels accords to the one of the other thylakoid protein complexes. In the light of the high susceptibility of ATPases to oxidative damage (Polizio et al ., 1999; Souza‐Santos et al ., 2001; Tamarit et al ., 1998), an increase in photo‐oxidative stress (see above) might destabilize the thylakoid ATP synthase and enhance its degradation during the non‐denaturing polyacrylamide gel separation.…”

Section: Discussionmentioning

confidence: 99%

The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana

et al. 2002

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SummaryThe mutants irt1-1 and irt1-2 of Arabidopsis thaliana were identi®ed among a collection of T-DNA-tagged lines on the basis of a decrease in the effective quantum yield of photosystem II. The mutations responsible interfere with expression of IRT1, a nuclear gene that encodes the metal ion transporter IRT1. In irt1 mutants, photosensitivity and chlorophyll¯uorescence parameters, as well as abundance and composition of the photosynthetic apparatus, are signi®cantly altered. Additional effects of the mutation under greenhouse conditions, including chlorosis and a drastic reduction in growth rate and fertility, are compatible with a de®ciency in iron transport. Propagation of irt1 plants on media supplemented with additional quantities of iron salts restores almost all aspects of wild-type behaviour. The irt2-1 mutant, which carries an En insertion in the highly homologous IRT2 gene of Arabidopsis thaliana, was identi®ed by reverse genetics and shows no symptoms of iron de®ciency. This, together with the ®nding that irt1-1 can be complemented by 35S::IRT1 but not by 35S::IRT2, demonstrates that, although the products of the two genes are closely related, only AtIRT1 is required for iron homeostasis under physiological conditions.

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Section: Discussionmentioning

confidence: 99%

The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana

et al. 2002

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“…Iron ions are bound in the enzymes in a redox-active form, as they react with H 2 O 2 giving rise to enzyme inactivation of F 1 ATPase from mitochondria and bacteria (5,6), as well as of the whole ATPsynthase (7). Evidence has been provided that ATPsynthase is a very sensitive target of iron-mediated oxidative attack in intact cells.…”

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confidence: 99%

Fe(III) Binding to Bacillus PS3 F1ATPase, αβ Subcomplexes and Isolated α- and β-Subunits

Contessi

Bald

Bäeuerlein

et al. 2001

Biochemical and Biophysical Research Communications

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“…Iron bound in this site mediates the H 2 O 2 ‐induced inactivation of both the bacterial [6] and mitochondrial enzyme [8] and evidence has been obtained for the enzyme inactivation even upon exposure to H 2 O 2 of the whole F 0 F 1 ‐ATP synthase [9] or of intact cells [10]. Nevertheless, just as occurs for the metal cofactor Mg(II) [11,12], a structural and functional role of iron may be hypothesised.…”

Section: Introductionmentioning

confidence: 99%

Effects of Fe(III) binding to the nucleotide‐independent site of F₁‐ATPase: enzyme thermostability and response to activating anions

Contessi¹,

Tanfani²,

Scirè³

et al. 2001

FEBS Letters

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Mitochondrial F 1 -ATPase was induced in different conformations by binding of specific ligands, such as nucleotides. Then, Fourier transform infrared spectroscopy (FT-IR) and kinetic analyses were run to evaluate the structural and functional effects of Fe(III) binding to the nucleotide-independent site. Binding of one equivalent of Fe(III) induced a localised stabilising effect on the F 1 -ATPase structure destabilised by a high concentration of NaCl, through rearrangements of the ionic network essential for the maintenance of enzyme tertiary and/or quaternary structure. Concomitantly, a lower response of ATPase activity to activating anions was observed. Both FT-IR and kinetic data were in accordance with the hypothesis of the Fe(III) site location near one of the catalytic sites, i.e. at the K K/L L subunit interface. ß 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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EPR Detection of Protein-Derived Radicals in the Reaction of H2O2 with Fe Bound in Mitochondrial F1ATPase

Cited by 6 publications

References 35 publications

The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana

The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana

Fe(III) Binding to Bacillus PS3 F1ATPase, αβ Subcomplexes and Isolated α- and β-Subunits

Effects of Fe(III) binding to the nucleotide‐independent site of F₁‐ATPase: enzyme thermostability and response to activating anions

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EPR Detection of Protein-Derived Radicals in the Reaction of H2O2 with Fe Bound in Mitochondrial F1ATPase

Cited by 6 publications

References 35 publications

The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana

The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana

Fe(III) Binding to Bacillus PS3 F1ATPase, αβ Subcomplexes and Isolated α- and β-Subunits

Effects of Fe(III) binding to the nucleotide‐independent site of F1‐ATPase: enzyme thermostability and response to activating anions

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Effects of Fe(III) binding to the nucleotide‐independent site of F₁‐ATPase: enzyme thermostability and response to activating anions