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Regulation of the redox potential of general acyl-CoA dehydrogenase by substrate binding by Nancy Donnelly Lenn; Marian T. Stankovich; Hung Wen Liu is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Regulation of the redox potential of general acyl-CoA dehydrogenase by substrate binding about?

Significant thermodynamic changes have been observed for general acyl-CoA dehydrogenase (GAD) upon substrate binding. Spectroelectrochemical studies of GAD and several of its substrates have revealed that these substrates are essentially isopotential for chain lengths of C-4 to C-16 (E 0' =-0.038 to -0.045 V vs SHE). When GAD is bound by these substrates, a dramatic shift in the midpoint potential of the enzyme is observed (E 0' = -0.136 V for ligand-free GAD and -0.026 V for acyl-CoA-bound GAD), thus allowing a thermodynamically favorable transfer of electrons from substrate to enzyme. This contrasts with values reported elsewhere. From these data an isopotential scheme of electron delivery into the electron-transport chain is proposed.

Who reads Regulation of the redox potential of general acyl-CoA dehydrogenase by substrate binding?

Author

Nancy Donnelly Lenn; Marian T. Stankovich; Hung Wen Liu

Publisher

American Chemical Society (ACS)

Published

1990

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)