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Contents

1 Background
2 Structure of ATP synthase
3 Electron Transfer
4 Oxygen Evolution
5 3D structures of photosystem II
6 Additional Resources
7 References

Background

ATP synthesis is the most prevalent chemical reaction in the biological world and ATP synthase is one of the most ubiquitous, abuntant proteins on earth. From Escherichia coli to plants and mammals, this enzyme is one of the most conserved during evolution[1].The molecular study of ATP synthase was initiated in 1960 when Efraim Racker and his colleagues reported thia isolation of soluable factor from beef heart mitochondria. ATP synthase produces ATP from adenosine diphosphate (ADP) and inorganic phosphate with the use of energy from a transmembrane proton-motive force generated by respiration or photosynthase[2].

Structure of ATP synthase

Strucutre of ATP synthases are basically similiar whatever the source. In their simplest form in prokaryotes, they contain eight different subunits, with stoichiometry α3β3γδεab2c10-14. The total molecular size is about 530kDa[3]. The enzyme consists of the extramembranous F1 catalytic domain linked by means of a central stalk to an intrinsic membrane domain called F0. In the atomic structure Of F1, the α and β subunits are arranged alternately around a coiled coil of two antiparallel α helices in the γ subunit. The catalytic sites are in the β subunits at the α/β subunit interface. The remainder of the γ subunit protrudes from the α3β3 assembly and can be cross linked to the polar loop region of the c subunits in F0. In mitochondria, the δ and ε subunits are associated with the γ subunit in the central stalk assembly, as are the bacterial and chloroplast ε subunits, the counterparts of mitochondrial δ. ATP-dependent rotation of γ and ε within an immobilized α3β3 complex from the thermophilic bacterium Bacillus PS3 has been observed directly.

[1] ATP synthase-a marvellous [2] Molecular Architecture of the rotary motor in ATP synthase [3] The molecular mechanism of ATP