Effects of large anphiphilic ligands upon the spectra and kinetics of cytochrome C oxidase

Cytoch ro me c oxidase (ferrocytochrome c : 02 oxidoreductase ; EC 1.9. 3.1) is the terminal enzyme in the mitochondrial electron transport chain, catalyzing the transfer of electrons from ferrocytochrome c to molecular oxygen. The effects of two large amphiphilic molecules - valinomycin and dibucaine upon the spectra of the isolated enzyme and upon the activity of both isolated enzyme and enzyme in membrane systems are investigated by using spectrophotometric and oxygen electrode techniques. The results show that both valinomycin and dibucaine change the Soret region of the speetrum and cause a partial inhibition in a concentration range higher than that in which they act as ionophores. It is concluded that both valinomycin and dibucaine binding induce a conformational change of the protein structure which modifies the spectrum of the a3 CUB centre and diminishes the rate of electron transfer between cytochrome a and the binuclear centre.

Letter - E.C. Schmon to Arthur A. Schmon, 25 & 26 October 1918

This letter discusses a piece of furniture Mrs. Schmon is debating whether to acquire. The letter is labelled number 180.

Letter - E.C. Schmon to Arthur A. Schmon, 20 July 1918

Eleanore Celeste mentions outings with her friend Hilda. She also mentions the list of promotions that she watches for Arthur's name. The letter is labelled number 130.

Letter to Joseph A. Woodruff from E.C. Thomas

Letter to Joseph A. Woodruff from E.C. Thomas saying that he intends to send the money which is owed to Mr. Woodruff, Dec. 4, 1865.