Title : Identification of dimethylbenzimidazole axial coordination and characterization of (14)N superhyperfine and nuclear quadrupole coupling in Cob(II)alamin bound to ethanolamine deaminase in a catalytically-engaged substrate radical-Cobalt(II) biradical state.

Pub. Date : 1999 Sep 28

PMID : 10504238






2 Functional Relationships(s)
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1 The results identify the coenzyme"s on-board dimethylbenzimidazole moiety as the alpha-axial ligand to cob(II)alamin in ethanolamine deaminase in the substrate radical-Co(II) biradical catalytic intermediate state. 5,6-dimethylbenzimidazole mitochondrially encoded cytochrome c oxidase II Homo sapiens
2 A 14% increase in the isotropic hyperfine coupling of the remote dimethylbenzimidazole (14)N nucleus in enzyme-bound versus free base-on cob(II)alamin shows an enhanced delocalization of unpaired spin density from Co(II) onto the axial ligand, which would contribute to the acceleration of the cobalt-carbon bond cleavage rate in situ. 5,6-dimethylbenzimidazole mitochondrially encoded cytochrome c oxidase II Homo sapiens