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Title: Biochemical and structural analysis of the central stalk in F1-ATPase from bovine heart mitochondria
Author: Gibbons, C.
Awarding Body: University of Cambridge
Current Institution: University of Cambridge
Date of Award: 2001
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ATP synthase plays a central role in biological energy conversion. The mitochondrial enzyme is found in the inner membrane and comprises a membrane bound Fo sector containing the proton channel and a water-soluble F1 domain containing the catalytic sites. The F1 domain (subunit composition (αβ)3γδε)) is linked to the Fo domain (subunit composition a,b,c10-12) by two connections, a central stalk and a peripheral stalk. The central stalk is the key rotary element in the enzyme's catalytic mechanism and is made up from the γ-, δ- and ε-subunits. X-ray crystallographic information, from the bovine and yeast mitochondrial enzymes, shows the γ-subunit to penetrate the (α,β)3 domain of F1 and protrude beneath it to interact with a ring of c-subunits in the Fo membrane domain. In F1-ATPase, the central stalk is believed to rotate relative to the (α,β)3 domain during catalysis. This rotation was observed directly in enzyme from several bacterial sources. In the holoenzyme, the central stalk is thought to rotate as an ensemble with the ring of ten c-subunits during catalysis. In crystals of F1-ATPase inhibited with dicyclohexylcarbodiimide (DCCD), shrinkage of the unit cell caused more extensive lattice contacts. Consequently, the order of the central stalk was improved enabling its complete structure to be solved to 2.4 Å resolution. One DCCD molecule per F1-ATPase reacted with a glutamate residue at position 1999 in the β-DP-subunit.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available