The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins.
Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins.
D000214:Acyl Coenzyme A / Q000494:pharmacology; D042964:Acyl-CoA Dehydrogenase; D044944:Acyl-CoA Dehydrogenases / Q000378:metabolism*; D000818:Animals; D004227:Dithionite / Q000494:pharmacology; D005420:Flavoproteins / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D010084:Oxidation-Reduction; D013552:Swine
D000214:Acyl Coenzyme A; D005420:Flavoproteins; C034681:octanoyl-coenzyme A; D004227:Dithionite; D044944:Acyl-CoA Dehydrogenases; D042964:Acyl-CoA Dehydrogenase