Abstract
Enzymes can carry out effective rate accelerations by virtue of their ability to utilize substrate-channeling forces to act as a mechanochemical valve. Such a channeling process is treated quantitatively using the key aspects of the free energy landscape; the balance between substrate positioning and conformational changes reflects the severe geometric and electronic requirements for the relatively tight transition state. The observed kcat/KM of about 106 M–1 s–1 for PGH2 cyclization has been revealed to be brought about by bringing together two properly oriented reactants of substrate and enzyme regarding the magnitude significance of the contribution from outer- and inner-binding stereopopulation along the free-energy channeling pathway and thus shapes the cascade cyclization route, enforcing precise spatial and temporal control. The apparent constant kcat of many P450 reactions involving the heme catalytic cycle, which is often on the order of 101–102 s–1 and is usually attributed to compound 0 to comp...
Published Version
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