Published in J Bioenerg Biomembr on October 01, 2000
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. EMBO J (1982) 38.14
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature (1994) 15.84
Direct observation of the rotation of F1-ATPase. Nature (1997) 9.57
Molecular architecture of the rotary motor in ATP synthase. Science (1999) 6.37
Intersubunit rotation in active F-ATPase. Nature (1996) 2.71
Rotation of subunits during catalysis by Escherichia coli F1-ATPase. Proc Natl Acad Sci U S A (1995) 2.39
Catalytic mechanism of F1-ATPase. Biochim Biophys Acta (1997) 2.29
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. J Biol Chem (1993) 1.74
The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Structure (1997) 1.65
The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis. Proc Natl Acad Sci U S A (1998) 1.30
Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase. J Biol Chem (1984) 1.11
Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography. Proc Natl Acad Sci U S A (1999) 1.11
Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase. J Biol Chem (1993) 1.10
Mg2+ coordination in catalytic sites of F1-ATPase. Biochemistry (1998) 1.07
Further characterization of nucleotide binding sites on chloroplast coupling factor one. Biochemistry (1981) 0.94
Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP. J Biol Chem (1994) 0.91
Relationship of tightly bound ADP and ATP to control and catalysis by chloroplast ATP synthase. Biochemistry (1988) 0.91
Structure of the divalent metal ion activator binding site of S-adenosylmethionine synthetase studied by vanadyl(IV) electron paramagnetic resonance. Biochemistry (1984) 0.87
Site-directed mutagenesis of stable adenosine triphosphate synthase. Biochim Biophys Acta (1988) 0.87
Demonstration of a transitory tight binding of ATP and of committed P(i) and ADP during ATP synthesis by chloroplasts. Proc Natl Acad Sci U S A (1976) 0.87
Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1-ATPase, is located at the catalytic site of the enzyme. FEBS Lett (1985) 0.86
Catalytic sites of Escherichia coli F1-ATPase. Characterization of unisite catalysis at varied pH. Biochemistry (1992) 0.85
Effects of nucleotides on the protein ligands to metals at the M2 and M3 metal-binding sites of the spinach chloroplast F1-ATPase. Biochemistry (1995) 0.83
Characterization of ligands of a high-affinity metal-binding site in the latent chloroplast F1-ATPase by EPR spectroscopy of bound VO2+. Biochemistry (1994) 0.82
Alkylation of cysteine 89 of the gamma subunit of chloroplast coupling factor 1 with N-ethylmaleimide alters nucleotide interactions. J Biol Chem (1994) 0.81
Coordination of nucleotides to metals at the M2 and M3 metal-binding sites of spinach chloroplast F1-ATPase. Biochemistry (1994) 0.81
Four tight nucleotide binding sites of chloroplast coupling factor 1. J Biol Chem (1991) 0.79
The role of tightly bound ADP on chloroplast ATPase. J Biol Chem (1985) 0.79
EPR spectroscopy of VO2+-ATP bound to catalytic site 3 of chloroplast F1-ATPase from Chlamydomonas reveals changes in metal ligation resulting from mutations to the phosphate-binding loop threonine (betaT168). J Biol Chem (1999) 0.78
Metal ligation by Walker homology B aspartate betaD262 at site 3 of the latent but not activated form of the chloroplast F(1)-ATPase from Chlamydomonas reinhardtii. J Biol Chem (1999) 0.78
The effects of sulfite or nitrate on turnover-dependent inhibition in the ATPase from Halobacterium saccharovorum are related to the binding of the second metal ion. Biochemistry (1993) 0.78
Characterization of the metal binding environment of catalytic site 1 of chloroplast F1-ATPase from Chlamydomonas. Biochemistry (2000) 0.77
Influence of divalent cations on nucleotide exchange and ATPase activity of chloroplast coupling factor 1. Biochemistry (1998) 0.77
Catalytic and EPR studies of the beta E204Q mutant of the chloroplast F1-ATPase from Chlamydomonas reinhardtii. Biochemistry (1996) 0.77