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Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
TLDR
In fungi, eubacteria, and plant chloroplasts, ring sizes of c10–c15 subunits have been observed, implying that these enzymes need 3.3–5 protons to make each ATP, but until now no higher eukaryote has been examined.
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Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols
The structures of F1-ATPase from bovine heart mitochondria inhibited with the dietary phytopolyphenol, resveratrol, and with the related polyphenols quercetin and piceatannol have been determined at…
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The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
TLDR
The central stalk in ATP synthase is made of γ, δ and ɛ subunits in the mitochondrial enzyme, and with crystals of F1-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed.
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The structure of bovine F1-ATPase in complex with its regulatory protein IF1
TLDR
In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1, which implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.
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Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
TLDR
Cryo-EM data was used to determine the fold of the a subunit, suggesting a proton translocation path through the Fo region that involves both the a and b subunits, and a Brownian ratchet mechanism for proton-translocation driven rotation in ATP synthases.
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Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution
TLDR
The structure of the intact ATP synthase from the α-proteobacterium Paracoccus denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by X-ray crystallography at 4.0 Å resolution and has provided deep insights into the workings of this extraordinary molecular machine.
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Ground State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 Å Resolution*
TLDR
The structure with bound azide represents the ADP inhibited state of the enzyme, and the new structure represents a ground state intermediate in the active catalytic cycle of ATP hydrolysis.
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How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria
The structure of bovine F1-ATPase inhibited by a monomeric form of the inhibitor protein, IF1, known as I1–60His, lacking most of the dimerization region, has been determined at 2.1-Å resolution. The…
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The structure of bovine F1‐ATPase inhibited by ADP and beryllium fluoride
TLDR
In the structure of F1‐ATPase with five bound ADP molecules (three in α‐subunits, one each in the βTP and βDP subunits), which has been determined, the conformation of αArg373 suggests that it senses the presence (or absence of the γ‐phosphate of ATP.
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How azide inhibits ATP hydrolysis by the F-ATPases.
TLDR
The structure of bovine F1-ATPase determined at 1.95-A resolution with crystals grown in the presence of ADP, 5'-adenylyl-imidodiphosphate, and azide explains the stimulatory effect of azide on ATP-sensitive potassium channels by enhancing the binding ofADP.
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