Crystal structure analysis of bovine heart cytochromecoxidase

Le résumé fourni par la source

MACROMOLECULES C-171 accessible faces and the three four-stranded !3-sheets.One therefore might characterize tllis fold as an inside-out ex!~ bmTell.TI1e present structure reflects the open confmmation of tl1e enzyme.vVe assume that lmge confcJimational changes upon catalysis are mediated mainly tl1rough two residues, a lysin and an m•ginine, which me located in the cleft between tl1e two domains.These residues assure tl1e open confmmation of the native enzyme by the repulsive force between the positive chmges of two anlino groups.The binding of one of tl1e two substrates probably results in neutralizing the repulsion between the two domains tl1ereby allowing the movement of a catalytically active cystein towmd tl1e cleft.PS04.07.20

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