Biochemistry Cover

Biochem Cover

The crystal structure of choline oxidase provides mechanistic insights and reveals a novel FAD C4a-adduct. The solvent accessible surfaces of the homodimeric enzyme are colored to illustrate the dimer interface and the major domains within one subunit. The FAD binding (blue) and substrate binding (green) domains are partially separated by a loop (orange) that sequesters the active site within the interior of the enzyme

Citation: 

*Quaye, O., *Lountos, G.T., Fan, F., Orville, A.M., and Gadda, G. (2008). Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase. Biochemistry 47: 243-256. * authors contributed equally

Published Date: 
January, 2008