Carboxybiotin translocation mechanisms suggested by diffraction studies of biotin and its vitamers.

Abstract
Biotin is a coenzyme that fixes CO2 for transfer in a family of carboxylase, decarboxylase and transcarboxylase enzymes. Their enzyme reactions involve 2 basic steps during which a carboxybiotinyl intermediate forms at 1 site and translocates to a 2nd (distinct) site for CO2 transfer. Diffraction studies of biotin and its vitamers suggest that translocation involves rotation about 1, or at most 2, bonds in biotin''s valeryl chain. The rotations are energetically economical gauche .dblarw. trans rotations about the 2 valeryl bonds nearest the biotin bicyclic ring. They move a C atom of a CO2 moiety bound at N-1'' approximately 7 .ANG., a distance in accord with spectroscopic measurements of 1 of the biotin enzymes. S in biotin may impart to the valeryl chain a conformational variability necessary for bond rotation and, hence, translocation between catalytic sites.