by National Academy of Sciences of the United States of America8c2001. in Washington, D.C .
Written in English
|Other titles||Proceedings of the National Academy of Sciences of the United States of America.|
|Statement||Satoshi P. Tsunoda ... [et al.].|
|Contributions||Tsunoda, Satoshi P., National Academy of Sciences (U.S.)|
Request PDF | Rotation of the c-subunit oligomer in fully functional F1F0 ATP synthase | The F(1)F(o)-type ATP synthase is the smallest motor enzyme known. Previous studies had established that. The F1Fo-type ATP synthase is the smallest motor enzyme known. Previous studies had established that the central γ and ɛ subunits of the F1 part rotate relative to a stator of α3β3 and δ subunits during catalysis. We now show that the ring of c subunits in the Fo part moves along with the γ and ɛ subunits. Mechanical Rotation of the c Subunit Oligomer in ATP Synthase (F 0F 1): Direct Observation Yoshihiro Sambongi,1 Yuko Iko,1 Mikio Tanabe,1 Hiroshi Omote,1* Atsuko Iwamoto-Kihara,2 Ikuo Ueda,1 Toshio Yanagida,3 Yoh Wada,1 Masamitsu Futai1† F 0F 1, found in mitochondria or bacterial membranes, synthesizes adenosine 5 The proton-transporting ATP synthase, F 0 F 1, consists of a catalytic sector, F 1 or F 1 –adenosine triphosphatase (ATPase) (α 3 β 3 γ 1 δ 1 ɛ 1), and a proton pathway, F 0 (a 1 b 2 c 12) (1, 2).The crystal structure of the bovine α 3 β 3 γ complex indicates that the α and β subunits are arranged alternately around the NH 2 - and COOH-terminal α helices of the γ subunit ().
F o and F 1 motors of ATP synthase. Schematic images of F o F 1-ATP rotor and stator parts are shown in red and blue, respectively. The subunit composition of bacterial F o is ab 2 c 10–15 (the number of c subunits varies from 10 to 15 in different species). F o is embedded in the cell membrane and rotates the c-ring against the ab 2 stator, driven by passive proton. Rotation of the c subunit oligomer in fully functional F 1 F 0 ATP synthase. Proc. Natl. Acad. Sci. U. S. A. ; View in Article. F o F 1 ‐ATP synthase mediates coupling of proton flow in F o and ATP synthesis/hydrolysis in F 1 through rotation of central rotor subunits. A ring structure of F o c subunits is widely believed to be a part of the rotor. Using an attached actin filament as a probe, we have observed the rotation of the F o c subunit ring in detergent‐solubilized F o F 1 ‐ATP synthase purified from. Y. Sambongi, et ical rotation of the c subunit oligomer in ATP synthase (F 0 F 1): direct observation Science, (), pp. Google Scholar.
F1F0 ATP synthases generate ATP by a rotary catalytic mechanism in which H+ transport is coupled to rotation of an oligomeric ring of c subunits extending through the membrane. Protons bind to and then are released from the aspartyl‐61 residue of subunit c at the center of the membrane. Subunit a of the F0 sector is thought to provide proton access channels to and from aspartyl‐ Tsunoda SP, Aggeler R, Yoshida M, Capaldi RA (b) Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase. Proc Natl Acad Sci U S A – Google Scholar Turina P, Samoray D and Gräber P () H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes. subunit c oligomer in the F1F0 ATP synthase: Subunit rotation of ATP synthase embedded in mem- tion of the c subunit oligomer in fully functional F1Fo ATP. The proton channel in ATP synthase is believed to lie at the interface of subunit a and the c oligomer. Protons enter the F 0 ‐complex from outside the cell through the periplasmic half‐channel and protonate the carboxyl group of a conserved glutamate or aspartate residue (Asp‐61 in E. coli) located in the subunit c, approximately.