Certain aspects of electron and coupled energy transfer in cardiac muscle Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/v979v5739

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  • The first area of investigation involves the electron transport of sub-mitochondrial particles and their components. The second area is the synthesis of ATP and other energy linked reactions and components of the energy conservation and transfer apparatus. Investigations on the nature of the tetramethyl-p-phenylenediamine (TMPD) shunt indicated that tetrachlorohydroquinone (TCHQ) as well as TMPD was able to overcome inhibition of succinate oxidase by antimycin A and quinoline-N-oxide but not thenoyltrifluoroacetone (TTA). TCHQ and TMPD also overcame inhibition of NADH oxidase by rotenone, antimycin A and quinoline-N-oxide. Kinetic studies indicated that exogenous cytochrome c greatly facilitated interaction of TMPD and TCHQ possibly by generating new pathways of electron transfer. Determination of kinetic constants for the process of restoration indicated that one site of oxidation and one site of reduction existed for TMPD with succinate oxidase. The TCHQ restoration was complicated by an inhibition of succinate oxidase that was greatly potentiated by exogenous cytochrome c. TMPD seems to interact at two sites of reduction with NADH oxidase while TCHQ has only one site of reduction. Both have single sites of oxidation. The effects of TCHQ and TMPD were also examined with NADH oxidase, succinate oxidase and cytochrome c oxidase. The site of action of TTA was investigated using the catalytic activities of the Keilin-Hartree heart muscle preparation (HMP) and soluble succinate dehydrogenases. The TTA apparently acts at a site which is closely related with the binding of the succinate dehydrogenase flavoprotein to the remainder of the chain. In addition, a new catalytic property of reconstitutively active succinate dehydrogenase was found: A "low K[subscript m]" succinate ferricyanide reductase. The interaction of cationic and neutral, stable free radicals was examined with the respiratory chain and a variety of soluble oxidation-reduction enzymes. The catalytic reduction of the stable free radical, Wurster's blue, seems to depend on flavoprotein oxidation-reduction enzymes. The properties of the adenosine triphosphatase of HMP were investigated in situ and in solution. The soluble enzyme from HMP was purified and, using nossal particles, its ability to participate in oxidative phosphorylation was demonstrated. A factor was isolated (alkali extractable soluble factor, AESF) which was found to be capable of restoring oxidative phosphorylation to several non-phosphorylating sub-mitochondrial particles. The relation of the AESF and oligomycin stimulation of the energy linked processes was investigated with HMP. The AESF was also able to stimulate the energy linked transhydrogenase of HMP. The properties of the factors were investigated as well as the interaction between the soluble AESF and the particulate respiratory assembly.
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