Professor Edward Slater FRS

Edward Slater made important contributions to the identification and understanding of the physiological role of the components of the respiratory chain, especially of the various cytochrome b complexes, iron–sulfur proteins and other iron-containing substances. He showed that the binding of certain inhibitors of oxidative phosphorylation acting at different sites (antimycin on electron transport, oligomycin on the coupling between electron transport and oxidative phosphorylation, and aurovertin in the ATP-synthesising enzyme) can be positively cooperative, and that the degree of cooperativity depends on the state of the mitochondrial membrane. He also demonstrated negative cooperative binding of a ligand to an enzyme (NAD to glyceraldehyde phosphate dehydrogenase); this has important implications for the mechanisms of cooperative binding generally.

Professor Edward Slater FRS died on 26 March 2016.

Biographical Memoir

Subject groups

  • Molecules of Life

    Biochemistry and molecular biology

Professor Edward Slater FRS
Elected 1975