Single Particle Analysis of ATP Synthase
نویسندگان
چکیده
منابع مشابه
Spotlighting motors and controls of single FoF1-ATP synthase.
Subunit rotation is the mechanochemical intermediate for the catalytic activity of the membrane enzyme FoF1-ATP synthase. smFRET (single-molecule FRET) studies have provided insights into the step sizes of the F1 and Fo motors, internal transient elastic energy storage and controls of the motors. To develop and interpret smFRET experiments, atomic structural information is required. The recent ...
متن کاملATP synthase
All living species use ATP as a general source of energy by hydrolysing it into ADP and phosphate. In most species the regeneration of this vital molecule is catalysed by the H+-transporting F1F0 ATP synthases, marvellous machines that couple the flow of protons down an electrochemical gradient to form ATP from ADP and phosphate. Under certain circumstances these enzymes can also work in the re...
متن کاملATP synthase: from single molecule to human bioenergetics
ATP synthase (F(o)F(1)) consists of an ATP-driven motor (F(1)) and a H(+)-driven motor (F(o)), which rotate in opposite directions. F(o)F(1) reconstituted into a lipid membrane is capable of ATP synthesis driven by H(+) flux. As the basic structures of F(1) (alpha(3)beta(3)gammadeltaepsilon) and F(o) (ab(2)c(10)) are ubiquitous, stable thermophilic F(o)F(1) (TF(o)F(1)) has been used to elucidat...
متن کاملQuick guide: ATP synthase
denotes the soluble catalytic headgroup where ATP synthesis and hydrolysis occur, and F o is the ion-translocating membrane domain (see Figure). What is it? An enzyme that uses energy from the transmembrane proton electrochemical gradient, generated by oxidative metabolism or photosynthesis, to produce ATP from ADP and P i. The enzyme can also act in reverse, hydrolysing ATP and pumping H + or ...
متن کاملATP-driven stepwise rotation of FoF1-ATP synthase.
FoF1-ATP synthase (FoF1) is a motor enzyme that couples ATP synthesis/hydrolysis with a transmembrane proton translocation. F1, a water-soluble ATPase portion of FoF1, rotates by repeating ATP-waiting dwell, 80 degrees substep rotation, catalytic dwell, and 40 degrees -substep rotation. Compared with F1, rotation of FoF1 has yet been poorly understood, and, here, we analyzed ATP-driven rotation...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2018
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.58.248