Abstract
An orbital perturbation approach of enzymatic catalysis is proposed. Orbital symmetry restrictions to a fast reaction pathway is lifted by first order perturbation of the catalyst potential. The drastic decrease of the energy gap is a second order effect enhance by the band-like structure of the enzymes. The model incorporates conformational specify and signals the importance of the low symmetries of the active sites. It is proposed that allosteric effects are due to shifts of the enzyme band structure.
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