Pages that link to "Q70533608"

The following pages link to 4-Azido-2-nitrophenyl phosphate, a new photoaffinity derivative of inorganic phosphate. Study of its interaction with the inorganic phosphate binding site of beef heart mitochondrial adenosine triphosphatase (Q70533608):

Displaying 16 items.

• p-Azidophenyl phosphate is a photoactivatable phosphorylating reagent and p-benzoquinone monoimine precursor (Q30667128) (← links)
• Natural and azido fatty acids inhibit phosphate transport and activate fatty acid anion uniport mediated by the mitochondrial phosphate carrier (Q31583143) (← links)
• The ATP synthase (F0-F1) complex in oxidative phosphorylation (Q35875025) (← links)
• ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas (Q36995302) (← links)
• 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 (Q37682248) (← links)
• The proton-ATPase of bacteria and mitochondria (Q40107164) (← links)
• Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches (Q40115807) (← links)
• Recent developments on structural and functional aspects of the F1 sector of H+-linked ATPases (Q40116822) (← links)
• Intrinsic tryptophan fluorescence of Schizosaccharomyces pombe mitochondrial F1-ATPase. A powerful probe for phosphate and nucleotide interactions (Q50804378) (← links)
• Photolabeling of the phosphate binding site of chloroplast coupling factor 1 with [32P]azidonitrophenyl phosphate (Q67575973) (← links)
• Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase (Q67897492) (← links)
• Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1-ATPase, is located at the catalytic site of the enzyme (Q69858872) (← links)
• Tightly bound nucleotides affect phosphate binding to mitochondrial F1-ATPase (Q69858877) (← links)
• [Use of chemical probes in the study of F1-ATPases] (Q69885565) (← links)
• Evidence that 4-azido-2-nitrophenylphosphate binds to the phosphate site on the β-subunit of Escherichia coli BF1 -ATPase (Q72777058) (← links)
• F1TPase of Escherichia coli: A mutation (uncA401) located in the middle of the α subunit affects the conformation essential for F1 activity (Q72806893) (← links)