Molecular Machines

ATP synthase

The 28 review prompts from the notes on ATP synthase. Answer each in your head, then reveal it. Your grade decides when the card comes back.

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Summary 7

Read this section: Summary, in the ATP synthase notes

  1. ATP synthase in mitochondria is driven by the blank across the inner membrane.

  2. In ATP synthase, protons crossing the membrane spin a ring of blank.

  3. Which ATP synthase subunit turns inside the α3β3 head and sets the state of each catalytic β subunit?

  4. One full turn of the ATP synthase rotor makes blank ATP, one per β subunit.

  5. Across species, the ATP synthase c-ring has blank c subunits.

  6. How does the tuberculosis drug bedaquiline stop the mycobacterial ATP synthase?

  7. Why would an engineered ATP synthase with a higher H+/ATP ratio (up to 5.8) be useful?

How it works 8

Read this section: How it works, in the ATP synthase notes

  1. Why can a proton not slip straight across subunit a of ATP synthase?

  2. Why can only a protonated site on the ATP synthase c-ring turn into the membrane lipid?

  3. In ATP synthase, each 120° turn of γ moves every β subunit blank.

  4. In ATP synthase, a β site takes up ADP and phosphate while open, and ATP forms when the site closes blank.

  5. In ATP synthase, which part of the catalytic cycle uses most of the proton energy?

  6. How can an 8-subunit c-ring drive an ATP synthase head that works in three 120° steps?

  7. What does ATP synthase do when ATP is present but the proton gradient is weak?

  8. Why does an ATP synthase with a c-ring of n subunits spend n/3 protons per ATP?

Big picture 5

Read this section: Big picture, in the ATP synthase notes

  1. A person remakes about blank of ATP every day, most of it made by ATP synthase.

  2. Why must the ATP synthases of the heart make ATP as fast as the heart uses it?

  3. One mitochondrial ATP synthase turning about 100 times per second makes about blank ATP per second.

  4. Where does the water-turbine analogy for ATP synthase break down?

  5. How does the bacterial flagellar motor use a proton gradient differently from ATP synthase?

Evidence 8

Read this section: Evidence, in the ATP synthase notes

  1. How did Noji and colleagues (1997) first see the γ rotor of F1 (the ATP synthase head) turn?

  2. How did Yasuda and colleagues (1998) show that each 120° step of F1 in ATP synthase uses one ATP?

  3. In F1 of ATP synthase, how does the work done in one 120° step compare with the free energy of one ATP?

  4. What did Itoh and colleagues (2004) show by turning γ of isolated F1 with magnets in the synthesis direction?

  5. Each 120° step of the F1 rotor of ATP synthase splits into substeps of about blank.

  6. How did Watt and colleagues (2010) find that the animal ATP synthase c-ring has 8 subunits?

  7. How did Petersen and colleagues (2012) measure the H+/ATP ratio of ATP synthase in lipid vesicles?

  8. How do the measured H+/ATP ratios of yeast and chloroplast ATP synthase compare with the ratios from their c-ring sizes?

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