Cain, K (1976) The locus of action in trialkyl tin compounds in yeast mitochondria. PhD thesis, University of Warwick.

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Abstract

Trialkyl tin compounds have been shown to be potent inhibitors of the yeast mitochondrial OS-ATPase complex in both the membrane bound form and purified soluble preparation. Binding studies with 11^Sn labelled triethyl tin have shown that the inhibitory properties of triethyl tin are due to the presence of a high affinity binding site which is not competed for by oligomycin or venturicidin. Die concent­ration of the binding site in the purified enzyme is 6mole/mole enzyme, the binding site has been shown to be located on the FQ component of the OS-ATPase complex.
A new radioactive affinity label (DBCT) for trialkyl tin compounds has been synthesized, binding experiments revealed that DBCT is a covalent inhibitor of the OS-ATPase. Extraction and isolation experi­ments have shown that DBCT binds to a small lipophilic, apparently non-protein component of the mitochondrial membrane. The significance of these findings are discussed in relation to current ideas on oxidative phosphorylation.
A biochemical genetic study has shown that triethyl tin may have another mode of action which is related to the transport of Adn nucleotides across the mitochondrial membrane.

Item Type:	Thesis (PhD)
Subjects:	Q Science > QD Chemistry
Library of Congress Subject Headings (LCSH):	Inorganic compounds -- Synthesis, Mitochondria, Yeast, Bioenergetics
Official Date:	August 1976
Dates:	Date Event August 1976 Submitted
Institution:	University of Warwick
Theses Department:	Department of Chemistry
Thesis Type:	PhD
Publication Status:	Unpublished
Language:	eng

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