Abstract

Further studies of butyryl CoA dehydrogenase show that the enzyme forms tight complexes with long-wavelength absorption bands upon addition of α, β-unsaturated alicyclic carboxylic acyl CoA compounds. As in the straight chain series, the size of the acyl moiety is critical. The thiol portion by contrast determines neither whether a long-wavelength band is formed nor the wavelength of maximum absorption if such a band is present. It does however markedly affect the dissociation constant. Unusual features of the acid stability of the acyl CoA found on the native green form of the enzyme are also reported.

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