The chlorite adduct of aquacobalamin: contrast with chlorite dismutase

In the reaction of aquacobalamin (aquaCbl) with chlorite, a stable species is detected and assigned as a Co(III)–chlorite complex, Co(III)–OClO⁻. Its UV–Vis spectrum is almost identical to that of aquaCbl, except for some minor differences at ~ 430 nm; cyanide can eliminate and prevent these changes. The ¹H-NMR spectra reveal strong influences of chlorite on the B2 and B4 protons of the cobalt-bound dimethyl benzimidazole ligand. Together, the UV–Vis and NMR titrations suggest a Kd of 10 mM or higher for chlorite on Cbl. Resonance Raman spectra reveal minor changes in the spectrum of aquaCbl to chlorite—as well as a disappearance of the free chlorite signals, consistent with Cbl–chlorite complex formation. Corroboration for these interpretations is also offered from mass spectrometry and DFT calculations. This Co(III)–OClO⁻ complex would be a stable analogue of the first reaction intermediate in the catalytic cycle of chlorite dismutase, or in the reaction of chlorite with a number of other heme proteins. The differences in reactivity between Co(III) cobalamin and Fe(III) heme towards chlorite are analyzed and rationalized, leading to a reconciliation of experimental and computational data for the latter.