Fluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymatic mechanism of the mitochondrial F1-ATPase
The mechanism by which fluoride and aluminum or beryllium in combination with ADP inhibit beef heart mitochondrial F1-ATPase was investigated. The kinetics of inhibition depended on the nature of the anion present in the F1-ATPase assay medium. Inhibition required the presence of Mg2+ and developed more rapidly with sulfite and sulfate than with chloride, i.e., with anions which activate F1-ATPase activity. The ADP-fluorometal complexes were bound quasi-irreversibly to F1, and each mole of the inhibitory nucleotide-fluorometal complex was tightly associated with 1 mol of Mg2+. One mole of nucleotide-fluorometal complex was able to inhibit the activity of 1 mol of catalytic site in F1. Direct measurements of bound fluoride, aluminum, beryllium, and ADP indicated that the F1-bound ADP-fluorometal complexes are of the following types: ADP1A11F4, ADP1Be1F1, ADP1Be1F2, or ADP1Be1F3. Fluoroaluminates or fluoroberyllates are isomorphous to Pi, and the inhibitory nucleotide-fluorometal complexes mimicked transient intermediates of nucleotides that appeared in the course of ATP hydrolysis. On the other hand, each mole of fully inhibited F1, retained 2 mol of inhibitory complexes. The same stoichiometry was observed when ADP was replaced by GDP, a nucleotide which, unlike ADP, binds only to the catalytic sites of F1. These results are discussed in terms of a stochastic model in which the three cooperative catalytic sites of F1 function in interactive pairs.
Medienart: |
Artikel |
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Erscheinungsjahr: |
1991 |
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Erschienen: |
1991 |
Enthalten in: |
Zur Gesamtaufnahme - volume:30 |
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Enthalten in: |
Biochemistry - 30(1991), 19 vom: 14. Mai, Seite 4726-33 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Issartel, J P [VerfasserIn] |
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Themen: |
61D2G4IYVH |
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Anmerkungen: |
Date Completed 20.06.1991 Date Revised 13.06.2019 published: Print Citation Status MEDLINE |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM01808964X |
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100 | 1 | |a Issartel, J P |e verfasserin |4 aut | |
245 | 1 | 0 | |a Fluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymatic mechanism of the mitochondrial F1-ATPase |
264 | 1 | |c 1991 | |
336 | |a Text |b txt |2 rdacontent | ||
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500 | |a Date Completed 20.06.1991 | ||
500 | |a Date Revised 13.06.2019 | ||
500 | |a published: Print | ||
500 | |a Citation Status MEDLINE | ||
520 | |a The mechanism by which fluoride and aluminum or beryllium in combination with ADP inhibit beef heart mitochondrial F1-ATPase was investigated. The kinetics of inhibition depended on the nature of the anion present in the F1-ATPase assay medium. Inhibition required the presence of Mg2+ and developed more rapidly with sulfite and sulfate than with chloride, i.e., with anions which activate F1-ATPase activity. The ADP-fluorometal complexes were bound quasi-irreversibly to F1, and each mole of the inhibitory nucleotide-fluorometal complex was tightly associated with 1 mol of Mg2+. One mole of nucleotide-fluorometal complex was able to inhibit the activity of 1 mol of catalytic site in F1. Direct measurements of bound fluoride, aluminum, beryllium, and ADP indicated that the F1-bound ADP-fluorometal complexes are of the following types: ADP1A11F4, ADP1Be1F1, ADP1Be1F2, or ADP1Be1F3. Fluoroaluminates or fluoroberyllates are isomorphous to Pi, and the inhibitory nucleotide-fluorometal complexes mimicked transient intermediates of nucleotides that appeared in the course of ATP hydrolysis. On the other hand, each mole of fully inhibited F1, retained 2 mol of inhibitory complexes. The same stoichiometry was observed when ADP was replaced by GDP, a nucleotide which, unlike ADP, binds only to the catalytic sites of F1. These results are discussed in terms of a stochastic model in which the three cooperative catalytic sites of F1 function in interactive pairs | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 7 | |a Anions |2 NLM | |
650 | 7 | |a Adenosine Diphosphate |2 NLM | |
650 | 7 | |a 61D2G4IYVH |2 NLM | |
650 | 7 | |a Aluminum |2 NLM | |
650 | 7 | |a CPD4NFA903 |2 NLM | |
650 | 7 | |a Proton-Translocating ATPases |2 NLM | |
650 | 7 | |a EC 3.6.3.14 |2 NLM | |
650 | 7 | |a Beryllium |2 NLM | |
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650 | 7 | |a Fluorides |2 NLM | |
650 | 7 | |a Q80VPU408O |2 NLM | |
700 | 1 | |a Dupuis, A |e verfasserin |4 aut | |
700 | 1 | |a Lunardi, J |e verfasserin |4 aut | |
700 | 1 | |a Vignais, P V |e verfasserin |4 aut | |
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