The energy transmission in ATP synthase: From the γ-c rotor to the α3β3 oligomer fixed by OSCP-b stator via the ... View Full Text


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Article Info

DATE

1996-10

AUTHORS

Yasuo Kagawa, Toshiro Hamamoto

ABSTRACT

ATP synthase (F0F1) is driven by an electrochemical potential of H+ (δΜH+). F0F1 is composed of an ion-conducting portion (F0) and a catalytic portion (F1). The subunit composition of F1 is α3β3γδε. The active α3β3 oligomer, characterized by X-ray crystallography, has been obtained only from thermnophilic F1 (TF1). We proposed in 1984 that ATP is released from the catalytic site (C site) by a conformational change induced by the βDELSEED sequence via γδε-F0. In fact, cross-linking of βDELSEED to γ stopped the ATP-driven rotation of γ in the center of α3β3. The torque of the rotation is estimated to be 420 pN·å from the δΜH+ and H+-current through F0F1. The angular velocity (Ω) of γ is the rate-limiting step, because δΜH+ increased theVmax of H+ current through F0, but not theKm(ATP). The rotational unit of F0 (=ab2c10) is π/5, while that in α3β3 is 2π/3. This difference is overcome by an analog-digital conversion via elasticity around βDELSEED with a threshold to release ATP. The αβ distance at the C site is about 9.6 å (2,8-diN3-ATP), and tight Mg-ATP binding in α3β3γ was shown by ESR. The rotational relaxation of TF1 is too rapid (Φ=100 nsec), but the rate of AT(D)P-induced conformational change of α3β3 measured with a synchrotron is close to Ω. The ATP bound between the P-loop and βE188 is released by the shift of βDELSEED from γRGL. Considering the viscosity resistance and inertia of the free rotor (γ-c), there may be a stator containing OSCP (=δ of TF1) and F0-d to hold free rotation of α3β3. More... »

PAGES

421-431

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02113984

DOI

http://dx.doi.org/10.1007/bf02113984

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021321730

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8951089


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