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Arch Biochem Biophys. 1999 Oct 1;370(1):138-41.

Ethanolamine ammonia-lyase has a "base-on" binding mode for coenzyme B(12).

Author information

1
Department of Biochemistry, University of Wisconsin, Madison, Wisconsin, 53705, USA.

Abstract

Ethanolamine ammonia-lyase (EAL, EC 4.3.1.7) catalyzes a coenzyme B(12)-dependent deamination of vicinal amino alcohols. The mode of binding of coenzyme B(12) to EAL has been investigated by electron paramagnetic resonance spectroscopy (EPR) using [(15)N]-dimethylbenzimidazole-coenzyme B(12). EAL was incubated with either unlabeled or (15)N-enriched coenzyme B(12) and then either exposed to light or treated with ethanol to generate the cleaved form of the cofactor, cob(II)alamin (B(12r)) bound in the active site. The reaction mixtures were examined by EPR spectroscopy at 77 K. (15)N superhyperfine splitting in the EPR signals of the low-spin Co(2+) of B(12r), bound in the active site of EAL, indicates that the dimethylbenzimidazole moiety of the cofactor contributes the lower axial ligand consistent with "base-on" binding of coenzyme B(12) to EAL.

PMID:
10496987
DOI:
10.1006/abbi.1999.1382
[Indexed for MEDLINE]

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