Ultrafast Transient Absorption Studies of Environment Influence on the Photolysis of B12 Complexes and the Subsequent Recombination and Escape of Caged Radicals.

Abstract

Femtosecond to nanosecond transient absorption experiments were performed on a series of B12 complexes to assess the influence of the solvent environment on the excited state electronic structure and resulting dynamics. A series of alkylcobalamins (adenosyl-, ethyl, methyl, and propylcobalamin), all of which are known to undergo cobalt-carbon bond homolysis in response to excitation at 400nm were studied in a variety of surroundings. Measurements on adenosylcobalamin (coenzyme B12) bound to glutamate mutase demonstrate a metal-to-ligand-charge-transfer (MLCT) state en route to bond homolysis, supported by protein influence on the excited state electronic structure. This charge transfer intermediate, which is similar to that reported in the literature for methylcobalamin, is not observed for free adenosylcobalamin. Measurements on methylcobalamin probe solvent influence on the MLCT state and characterize it by a large charge density transfer. This result is in contrast to studies on cyanocobalamin, which is not observed to undergo homolysis, where the solvent dependent lifetime of an intermediate ligand-to-metal-charge-transfer (LMCT) state is characterized by a modest transfer of charge density. Such a LMCT intermediate is observed for adenosylcobalamin in water leading to bond homolysis. The protein has greatly altered the photochemical pathway to homolysis, which is expected to be representative of influence on thermolysis. Upon homolysis the photoinduced alkyl and cob(II)alamin radicals may recombine or escape the solvent cage to form solvent separated radical pairs which do not recombine in the bulk by the 9ns time limit of these experiments. Recombination can be monitored directly via the oxidation state of the cobalt atom. The neutral alkyl radical is a paradigm for small particle escape and diffusive motion in a liquid. The escape behavior is similar for adenosyl, ethyl, and propyl radicals indicating that hydrogen bonding with the solvent is not a major influence. The methyl radical appears to dissociate from the cobalamin with excess kinetic energy. Preliminary analysis is presented suggesting the escape is not adequately modeled by the steady state diffusive hydrodynamic theory. To explain the discrepancy of escape in different environments an outline of planned analysis is presented.