Dataset Information

Efficient C-H Bond Activations via O₂ Cleavage by a Dianionic Cobalt(II) Complex.

ABSTRACT: A dianionic, square planar cobalt(II) complex reacts with O₂ in the presence of acetonitrile to give a cyanomethylcobalt(III) complex formed by C-H bond cleavage. Interestingly, PhIO and p-tolylazide react similarly to give the same cyanomethylcobalt(III) complex. Competition studies with various hydrocarbon substrates indicate that the rate of C-H bond cleavage greatly depends on the p Ka of the C-H bond, rather than on the C-H bond dissociation energy. Kinetic isotope experiments reveal a moderate KIE value of ca. 3.5 using either O₂ or PhIO. The possible involvement of a cobalt(IV) oxo species in this chemistry is discussed.

SUBMITTER: Nguyen AI

PROVIDER: S-EPMC4111274 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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Publications

Efficient C-H Bond Activations via O2 Cleavage by a Dianionic Cobalt(II) Complex.

Nguyen Andy I AI Hadt Ryan G RG Solomon Edward I EI Tilley T Don TD

Chemical science 20140701 7

A dianionic, square planar cobalt(II) complex reacts with O2 in the presence of acetonitrile to give a cyanomethylcobalt(III) complex formed by C-H bond cleavage. Interestingly, PhIO and p-tolylazide react similarly to give the same cyanomethylcobalt(III) complex. Competition studies with various hydrocarbon substrates indicate that the rate of C-H bond cleavage greatly depends on the p Ka of the C-H bond, rather than on the C-H bond dissociation energy. Kinetic isotope ...[more]

PMID: 25071930

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Project description:Protein contributions to the substrate-triggered cleavage of the cobalt-carbon (Co-C) bond and formation of the cob(II)alamin-5'-deoxyadenosyl radical pair in the adenosylcobalamin (AdoCbl)-dependent ethanolamine ammonia-lyase (EAL) from Salmonella typhimurium have been studied by using pulsed-laser photolysis of AdoCbl in the EAL-AdoCbl-substrate ternary complex, and time-resolved probing of the photoproduct dynamics by using ultraviolet-visible absorption spectroscopy on the 10(-7)-10(-1) s time scale. Experiments were performed in a fluid dimethylsulfoxide/water cryosolvent system at 240 K, under conditions of kinetic competence for thermal cleavage of the Co-C bond in the ternary complex. The static ultraviolet-visible absorption spectra of holo-EAL and ternary complex are comparable, indicating that the binding of substrate does not labilize the cofactor cobalt-carbon (Co-C) bond by significantly distorting the equilibrium AdoCbl structure. Photolysis of AdoCbl in EAL at 240 K leads to cob(II)alamin-5'-deoxyadenosyl radical pair quantum yields of <0.01 at 10(-6) s in both holo-EAL and ternary complex. Three photoproduct states are populated following a saturating laser pulse, and labeled, P(f), P(s), and P(c). The relative amplitudes and first-order recombination rate constants of P(f) (0.4-0.6; 40-50 s(-1)), P(s) (0.3-0.4; 4 s(-1)), and P(c) (0.1-0.2; 0) are comparable in holo-EAL and in the ternary complex. Time-resolved, full-spectrum electron paramagnetic resonance (EPR) spectroscopy shows that visible irradiation alters neither the kinetics of thermal cob(II)alamin-substrate radical pair formation, nor the equilibrium between ternary complex and cob(II)alamin-substrate radical pair, at 246 K. The results indicate that substrate binding to holo-EAL does not "switch" the protein to a new structural state, which promptly stabilizes the cob(II)alamin-5'-deoxyadenosyl radical pair photoproduct, either through an increased barrier to recombination, a decreased barrier to further radical pair separation, or lowering of the radical pair state free energy, or a combination of these effects. Therefore, we conclude that such a change in protein structure, which is independent of changes in the AdoCbl structure, and specifically the Co-C bond length, is not a basis of Co-C bond cleavage catalysis. The results suggest that, following the substrate trigger, the protein interacts with the cofactor to contiguously guide the cleavage of the Co-C bond, at every step along the cleavage coordinate, starting from the equilibrium configuration of the ternary complex. The cleavage is thus represented by a diagonal trajectory across a free energy surface, that is defined by chemical (Co-C separation) and protein configuration coordinates.

Dataset Information

Efficient C-H Bond Activations via O₂ Cleavage by a Dianionic Cobalt(II) Complex.

Publications

Efficient C-H Bond Activations <i>via</i> O<sub>2</sub> Cleavage by a Dianionic Cobalt(II) Complex.

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