1, 2 F-type ATP synthases are trans-membrane molecular rotary motors that perform the final step in these processes by harnessing the membrane potential to synthesize ATP in a rotary catalytic mechanism in a manner similar to the production of electricity in the generators of power plants ( Fig. 1). The majority of the ATP within cells is synthesized by utilizing a trans-membrane gradient of protons or sodium ions generated by either photosynthesis or respiration. ATP is synthesized in an energetically unfavorable phosphorylation reaction in which inorganic phosphate is added to adenosine-5′diphosphate (ADP).
#SKETCHUP WAREHOUSE ROTATING MECHANISM FREE#
Taken together these molecular snapshots show that nano-scale rotary engines have much in common with basic design principles of man made machines from the function of individual “machine elements” to the requirement of the right “fuel” and “oil” for different types of motors.Īll living cells require the multifunctional nucleotide adenosine-5′-triphosphate (ATP) both as a carrier of free energy to drive chemical reactions and molecular motion and also as a building block for DNA and RNA. Electron cryo-tomography has provided new insights into the supra-molecular arrangement of eukaryotic ATP synthases within mitochondria and mass-spectrometry has started to identify specifically bound lipids presumed to be essential for function.
Composite models of the intact F-, V- and A-type ATPases have been constructed by fitting high-resolution X-ray structures of individual subunits or sub-complexes into low-resolution electron densities of the intact enzymes derived from electron cryo-microscopy. Recent work has elucidated the general architecture and subunit compositions of all three sub-types of rotary ATPases. They either synthesize or hydrolyze the universal biological energy carrier adenosine triphosphate.
Rotary ATPases are molecular rotary motors involved in biological energy conversion.
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