Role of Subunits in Proton-Translocating ATPase (F0–F1)

Futai, Masamitsu; Kanazawa, Hiroshi

doi:10.1016/b978-0-12-152510-1.50011-0

Cited by 81 publications

(33 citation statements)

References 175 publications

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“…The FIF 0 ATPases of bovine mitochondria and Escherichia coli have many common structural feal tures (reviews [1][2][3][4][5]). They appear to be made up of a membrane-bound domain Fl which is attached to a transmembrane structure, F0.…”

Section: Introductionmentioning

confidence: 99%

Subunit equivalence in Escherichia coli and bovine heart mitochondrial F₁F₀ ATPases

1982

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Section: Introductionmentioning

confidence: 99%

Subunit equivalence in Escherichia coli and bovine heart mitochondrial F₁F₀ ATPases

1982

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confidence: 99%

“…Attempts to identify functional amino acids in the catalytic site have been carried out by using labeled chemical modifiers, known to interact with specific amino acid residues, that bind to the F1 ATPase and inactivate it. After dissociating the labeled enzyme complex to its individual subunits, the label was detected mainly on the p subunit (7,8).A detailed characterization of individual substrate binding sites and their possible identification with the catalytic site in the Fl-enzyme complex is difficult because of the complexity of its structure and function. It contains two or three copies of aB pairs, which could be in different conformational states in the catalytically active complex (17,18), and its activity leads to interconversion of the substrates.…”

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confidence: 99%

“…Elucidation of the mechanism of action of this enzyme complex requires a detailed description of its catalytic site. This includes identification of the catalytic subunit and characterization of substrate binding sites and essential amino acid residues on this subunit.A large number of studies using different approaches point to the p subunit as the one that contains the catalytic site and is involved in substrate binding (3,4,8). Thus, various studies have shown that the F1 sector has several nucleotide binding sites that reside in its two larger subunits, a and /3(4, 7, 9-11).…”

mentioning

confidence: 99%

“…A large number of studies using different approaches point to the p subunit as the one that contains the catalytic site and is involved in substrate binding (3,4,8). Thus, various studies have shown that the F1 sector has several nucleotide binding sites that reside in its two larger subunits, a and /3(4, 7, 9-11).…”

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Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated beta subunit of the F0.F1 ATP synthase is a catalytic site.

Khananshvili¹,

Gromet-Elhanan²

1985

Proc. Natl. Acad. Sci. U.S.A.

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complex is still unknown, although a number of mechanisms have been proposed (6, 7). Elucidation of the mechanism of action of this enzyme complex requires a detailed description of its catalytic site. This includes identification of the catalytic subunit and characterization of substrate binding sites and essential amino acid residues on this subunit.A large number of studies using different approaches point to the p subunit as the one that contains the catalytic site and is involved in substrate binding (3,4,8). Thus, various studies have shown that the F1 sector has several nucleotide binding sites that reside in its two larger subunits, a and /3(4, 7, 9-11). At least one Pi binding site has also been revealed in the F1 sector (12, 13), and from studies with a Pi analog it seems to be located on the p subunit (14-16). Attempts to identify functional amino acids in the catalytic site have been carried out by using labeled chemical modifiers, known to interact with specific amino acid residues, that bind to the F1 ATPase and inactivate it. After dissociating the labeled enzyme complex to its individual subunits, the label was detected mainly on the p subunit (7,8).A detailed characterization of individual substrate binding sites and their possible identification with the catalytic site in the Fl-enzyme complex is difficult because of the complexity of its structure and function. It contains two or three copies of aB pairs, which could be in different conformational states in the catalytically active complex (17,18), and its activity leads to interconversion of the substrates. These difficulties may be overcome if, instead of testing the whole F1 sector, isolated, purified, and reconstitutively active a and p subunits are used. Such subunits have been obtained so far only from three bacterial sources: a thermophilic bacterium (19), Escherichia coli (20), and Rhodospirillum rubrum (21). They are indeed a much simpler system for study as they show no subunit-subunit interactions and no catalytic activity by themselves, although they can restore ATP synthesis or hydrolysis (or both) to preparations that lack them (19-21).Direct binding studies with labeled substrates have been carried out only with the a subunit of E. coli (22) and the 8 subunit of R. rubrum (23,24,41). These studies have identified one nucleotide binding site on the a subunit (22), whereas the p subunit contained two binding sites for ATP (23) or ADP (24) and one binding site for Pi (41). One of the nucleotide binding sites on the p subunit is a Mg-dependent high-affinity site, which is very similar to the binding site located on the a subunit. The second is a Mg-dependent low-affinity site, which has been suggested to contain also the binding site for Pi, because both nucleotides have been found to be competitive inhibitors of Pi binding (41). Furthermore, Pi seems to bind at the site occupied by the yphosphate group of ATP, since ATP is a much more potent inhibitor of Pi binding to the p subunit than is ADP.In this study we attempt to identify ...

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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

Walker¹,

Saraste²,

Runswick³

et al. 1982

The EMBO Journal

5,064

3,296

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The a-and ,B-subunits of membrane-bound ATP synthase complex bind ATP and ADP: B contributes to catalyic sites, and a may be involved in regulation of ATP synthase activity. The sequences of ,B-subunits are highly conserved in Escherichia coli and bovine mitochondria. Also a and ( are weakly homologous to each other throughout most of their amino acid sequences, suggesting that they have common functions in catalysis. Related sequences in both a and (3 and in other enzymes that bind ATP or ADP in catalysis, notably myosin, phosphofructokinase, and adenylate kinase, help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.

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Role of Subunits in Proton-Translocating ATPase (F0–F1)

Cited by 81 publications

References 175 publications

Subunit equivalence in Escherichia coli and bovine heart mitochondrial F₁F₀ ATPases

Subunit equivalence in Escherichia coli and bovine heart mitochondrial F₁F₀ ATPases

Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated beta subunit of the F0.F1 ATP synthase is a catalytic site.

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

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Role of Subunits in Proton-Translocating ATPase (F0–F1)

Cited by 81 publications

References 175 publications

Subunit equivalence in Escherichia coli and bovine heart mitochondrial F1F0 ATPases

Subunit equivalence in Escherichia coli and bovine heart mitochondrial F1F0 ATPases

Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated beta subunit of the F0.F1 ATP synthase is a catalytic site.

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

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Subunit equivalence in Escherichia coli and bovine heart mitochondrial F₁F₀ ATPases

Subunit equivalence in Escherichia coli and bovine heart mitochondrial F₁F₀ ATPases