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

Erscheinungsjahr:

1991

Erschienen:

1991

Enthalten in:

Zur Gesamtaufnahme - volume:30

Enthalten in:

Biochemistry - 30(1991), 19 vom: 14. Mai, Seite 4726-33

Sprache:

Englisch

Beteiligte Personen:

Issartel, J P [VerfasserIn]
Dupuis, A [VerfasserIn]
Lunardi, J [VerfasserIn]
Vignais, P V [VerfasserIn]

Themen:

61D2G4IYVH
Adenosine Diphosphate
Aluminum
Anions
Beryllium
CPD4NFA903
EC 3.6.3.14
Fluorides
Journal Article
OW5102UV6N
Proton-Translocating ATPases
Q80VPU408O
Research Support, Non-U.S. Gov't

Anmerkungen:

Date Completed 20.06.1991

Date Revised 13.06.2019

published: Print

Citation Status MEDLINE

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM01808964X