Catalytic site occupancy during ATP synthase catalysis

An early proposal was that for rapid ATP synthesis by the rotational ATP synthase, a specific second site must bind ADP and Pi, and for rapid ATP hydrolysis a different second site must bind ATP. Such bi‐site activation was considered to occur whether or not an ADP or ATP was at a third site. In contrast, a more recent proposal is that rapid ATP hydrolysis requires that all three sites have bound ADP or ATP present. However, discovery that one second site binds ADP better than ATP, together with other data and considerations support the earlier proposal. The retention or rebinding of ADP can explain why three sites fill during hydrolysis as ATP concentration is increased although bi‐site activation still prevails.

[1]  A. Leslie,et al.  Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites Implications for the Mechanism of Rotary Catalysis , 2001, Cell.

[2]  P. Boyer,et al.  Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase. , 1998, The Biochemical journal.

[3]  A. Leslie,et al.  Structural model of F1-ATPase and the implications for rotary catalysis. , 2000, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[4]  J. Weber,et al.  Bi-site Catalysis in F1-ATPase: Does It Exist?* , 2001, The Journal of Biological Chemistry.

[5]  A G Leslie,et al.  Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride. , 2000, Structure.

[6]  A. Leslie,et al.  The structure and nucleotide occupancy of bovine mitochondrial F1‐ATPase are not influenced by crystallisation at high concentrations of nucleotide , 2001, FEBS letters.

[7]  P. A. Fortes,et al.  The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP. , 1998, Biochemistry.

[8]  Kazuhiko Kinosita,et al.  Direct observation of the rotation of F1-ATPase , 1997, Nature.

[9]  C. Bowman,et al.  Specific Tryptophan Substitution in Catalytic Sites of Escherichia coli F1-ATPase Allows Differentiation between Bound Substrate ATP and Product ADP in Steady-state Catalysis* , 1996, The Journal of Biological Chemistry.

[10]  W. Allison,et al.  Inhibitory Mg-ADP—Fluoroaluminate Complexes Bound to Catalytic Sites of F1-ATPases: Are They Ground-State or Transition-State Analogs? , 2000, Journal of bioenergetics and biomembranes.

[11]  Masasuke Yoshida,et al.  Cross-linking of Two β Subunits in the Closed Conformation in F1-ATPase* , 1999, The Journal of Biological Chemistry.

[12]  P. Boyer,et al.  Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase. , 1979, The Journal of biological chemistry.

[13]  P. Boyer,et al.  Interaction of mitochondrial F1-ATPase with trinitrophenyl derivatives of ATP and ADP. Participation of third catalytic site and role of Mg2+ in enzyme inactivation. , 1994, The Journal of biological chemistry.

[14]  J. Weber,et al.  F1-ATPase, Roles of Three Catalytic Site Residues* , 1997, The Journal of Biological Chemistry.

[15]  P. Boyer,et al.  The binding change mechanism for ATP synthase--some probabilities and possibilities. , 1993, Biochimica et biophysica acta.

[16]  R. L. Cross,et al.  Catalytic site occupancy during ATP hydrolysis by MF1-ATPase. Evidence for alternating high affinity sites during steady-state turnover. , 1988, The Journal of biological chemistry.

[17]  J. Weber,et al.  Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied. , 1993, The Journal of biological chemistry.

[18]  Jan Pieter Abrahams,et al.  Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria , 1994, Nature.

[19]  J. Weber,et al.  Catalytic mechanism of F1-ATPase. , 1997, Biochimica et biophysica acta.

[20]  P. Gräber,et al.  Kinetics of ATP synthesis catalyzed by the H(+)-ATPase from chloroplasts (CF0F1) reconstituted into liposomes and coreconstituted with bacteriorhodopsin. , 1992, European journal of biochemistry.

[21]  J. Weber,et al.  ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis. , 2000, Biochimica et biophysica acta.

[22]  P. Boyer,et al.  Evidence that energization of the chloroplast ATP synthase favors ATP formation at the tight binding catalytic site and increases the affinity for ADP at another catalytic site. , 1993, The Journal of biological chemistry.

[23]  W. Allison.  F1-ATPase: A Molecular Motor That Hydrolyzes ATP with Sequential Opening and Closing of Catalytic Sites Coupled to Rotation of Its γ Subunit , 1998 .

[24]  S. Ferguson,et al.  Kinetics of oxidative phosphorylation in Paracoccus denitrificans. 1. Mechanism of ATP synthesis at the active site(s) of F0F1-ATPase. , 1990, Biochemistry.

[25]  J. Weber,et al.  Effects of the Inhibitors Azide, Dicyclohexylcarbodiimide, and Aurovertin on Nucleotide Binding to the Three F1-ATPase Catalytic Sites Measured Using Specific Tryptophan Probes* , 1998, The Journal of Biological Chemistry.

[26]  W. Allison,et al.  Substitution of βGlu201 in the α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 Increases the Affinity of Catalytic Sites for Nucleotides* , 2000, The Journal of Biological Chemistry.

[27]  Hiroyasu Itoh,et al.  Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase , 2001, Nature.

[28]  P. Boyer,et al.  Toward an Adequate Scheme for the ATP Synthase Catalysis , 2001, Biochemistry (Moscow).