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Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | FEBS Letters, 373, 1995, 2, S. 141-145 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Lippe, Giovanna Di Pancrazio, Francesca Dabbeni-Sala, Federica Bertoli, Enrico Tanfani, Fabio Lippe, Giovanna Di Pancrazio, Francesca Dabbeni-Sala, Federica Bertoli, Enrico Tanfani, Fabio |
|---|---|
| author |
Lippe, Giovanna Di Pancrazio, Francesca Dabbeni-Sala, Federica Bertoli, Enrico Tanfani, Fabio |
| spellingShingle |
Lippe, Giovanna Di Pancrazio, Francesca Dabbeni-Sala, Federica Bertoli, Enrico Tanfani, Fabio FEBS Letters Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
lippe, giovanna |
| spelling |
Lippe, Giovanna Di Pancrazio, Francesca Dabbeni-Sala, Federica Bertoli, Enrico Tanfani, Fabio 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/0014-5793(95)01022-7 <jats:p>Mitochondrial F<jats:sub>1</jats:sub>ATPase from beef heart was treated with different buffers in order to modulate the nucleotide content of the enzyme and then analysed by FT‐IR spectroscopy. Treatment of F<jats:sub>1</jats:sub>ATPase with a buffer lacking nucleotides and glycerol led to the formation of two fractions consisting of an inactive aggregated enzyme deprived almost completely of bound nucleotides and of an active enzyme containing ATP only in the tight sites and having a structure largely accessible to the solvent and a low thermal stability. Treatment of F<jats:sub>1</jats:sub>ATPase with saturating ADP, which induced the hysteretic inhibition during turnover, or AMP‐PNP did not affect remarkably the secondary structure of the enzyme complex but significantly increased its compactness and thermal stability. It was hypothesised that the formation of the inactive aggregated enzyme was mainly due to the destabilisation of the α‐subunits of F<jats:sub>1</jats:sub>ATPase and that the induction of the hysteretic inhibition is related to a particular conformation of the enzyme, which during turnover becomes unable to sustain catalysis.</jats:p> Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F<sub>1</sub>ATPase: a Fourier transform infrared spectroscopic study FEBS Letters |
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| title |
Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_unstemmed |
Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_full |
Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_fullStr |
Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_full_unstemmed |
Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_short |
Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_sort |
influence of adp, amp‐pnp and of depletion of nucleotides on the structural properties of f<sub>1</sub>atpase: a fourier transform infrared spectroscopic study |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/0014-5793(95)01022-7 |
| publishDate |
1995 |
| physical |
141-145 |
| description |
<jats:p>Mitochondrial F<jats:sub>1</jats:sub>ATPase from beef heart was treated with different buffers in order to modulate the nucleotide content of the enzyme and then analysed by FT‐IR spectroscopy. Treatment of F<jats:sub>1</jats:sub>ATPase with a buffer lacking nucleotides and glycerol led to the formation of two fractions consisting of an inactive aggregated enzyme deprived almost completely of bound nucleotides and of an active enzyme containing ATP only in the tight sites and having a structure largely accessible to the solvent and a low thermal stability. Treatment of F<jats:sub>1</jats:sub>ATPase with saturating ADP, which induced the hysteretic inhibition during turnover, or AMP‐PNP did not affect remarkably the secondary structure of the enzyme complex but significantly increased its compactness and thermal stability. It was hypothesised that the formation of the inactive aggregated enzyme was mainly due to the destabilisation of the α‐subunits of F<jats:sub>1</jats:sub>ATPase and that the induction of the hysteretic inhibition is related to a particular conformation of the enzyme, which during turnover becomes unable to sustain catalysis.</jats:p> |
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| author | Lippe, Giovanna, Di Pancrazio, Francesca, Dabbeni-Sala, Federica, Bertoli, Enrico, Tanfani, Fabio |
| author_facet | Lippe, Giovanna, Di Pancrazio, Francesca, Dabbeni-Sala, Federica, Bertoli, Enrico, Tanfani, Fabio, Lippe, Giovanna, Di Pancrazio, Francesca, Dabbeni-Sala, Federica, Bertoli, Enrico, Tanfani, Fabio |
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| description | <jats:p>Mitochondrial F<jats:sub>1</jats:sub>ATPase from beef heart was treated with different buffers in order to modulate the nucleotide content of the enzyme and then analysed by FT‐IR spectroscopy. Treatment of F<jats:sub>1</jats:sub>ATPase with a buffer lacking nucleotides and glycerol led to the formation of two fractions consisting of an inactive aggregated enzyme deprived almost completely of bound nucleotides and of an active enzyme containing ATP only in the tight sites and having a structure largely accessible to the solvent and a low thermal stability. Treatment of F<jats:sub>1</jats:sub>ATPase with saturating ADP, which induced the hysteretic inhibition during turnover, or AMP‐PNP did not affect remarkably the secondary structure of the enzyme complex but significantly increased its compactness and thermal stability. It was hypothesised that the formation of the inactive aggregated enzyme was mainly due to the destabilisation of the α‐subunits of F<jats:sub>1</jats:sub>ATPase and that the induction of the hysteretic inhibition is related to a particular conformation of the enzyme, which during turnover becomes unable to sustain catalysis.</jats:p> |
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| imprint | Wiley, 1995 |
| imprint_str_mv | Wiley, 1995 |
| institution | DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1 |
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| language | English |
| last_indexed | 2024-03-01T14:58:10.069Z |
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| mega_collection | Wiley (CrossRef) |
| physical | 141-145 |
| publishDate | 1995 |
| publishDateSort | 1995 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | FEBS Letters |
| source_id | 49 |
| spelling | Lippe, Giovanna Di Pancrazio, Francesca Dabbeni-Sala, Federica Bertoli, Enrico Tanfani, Fabio 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/0014-5793(95)01022-7 <jats:p>Mitochondrial F<jats:sub>1</jats:sub>ATPase from beef heart was treated with different buffers in order to modulate the nucleotide content of the enzyme and then analysed by FT‐IR spectroscopy. Treatment of F<jats:sub>1</jats:sub>ATPase with a buffer lacking nucleotides and glycerol led to the formation of two fractions consisting of an inactive aggregated enzyme deprived almost completely of bound nucleotides and of an active enzyme containing ATP only in the tight sites and having a structure largely accessible to the solvent and a low thermal stability. Treatment of F<jats:sub>1</jats:sub>ATPase with saturating ADP, which induced the hysteretic inhibition during turnover, or AMP‐PNP did not affect remarkably the secondary structure of the enzyme complex but significantly increased its compactness and thermal stability. It was hypothesised that the formation of the inactive aggregated enzyme was mainly due to the destabilisation of the α‐subunits of F<jats:sub>1</jats:sub>ATPase and that the induction of the hysteretic inhibition is related to a particular conformation of the enzyme, which during turnover becomes unable to sustain catalysis.</jats:p> Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F<sub>1</sub>ATPase: a Fourier transform infrared spectroscopic study FEBS Letters |
| spellingShingle | Lippe, Giovanna, Di Pancrazio, Francesca, Dabbeni-Sala, Federica, Bertoli, Enrico, Tanfani, Fabio, FEBS Letters, Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_full | Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_fullStr | Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_full_unstemmed | Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_short | Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| title_sort | influence of adp, amp‐pnp and of depletion of nucleotides on the structural properties of f<sub>1</sub>atpase: a fourier transform infrared spectroscopic study |
| title_unstemmed | Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/0014-5793(95)01022-7 |