Binding sites of pyridine in cytochrome P-450cam.
Careful titration of oxidized cytochrome P-450cam from Pseudomonas putida with pyridine revealed deviations of the Eadie plot from linearity in the substrate-bound as well as in the substrate-free protein. A binding model which assumes two binding sites for pyridine--the iron and the camphor binding site--is able to describe completely the nonlinear Eadie plot.
Ristau
O
O
Central Institute of Molecular Biology, Department of Molecular Biophysics, Berlin, F.R.G.
Jung
C
C
D001665:Binding Sites; D019475:Camphor 5-Monooxygenase; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D011549:Pseudomonas / Q000201:enzymology; D011725:Pyridines / Q000737:chemistry*; D013816:Thermodynamics
D011725:Pyridines; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase; C023666:pyridine