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Heavy‐atom effects associated with methylmercury (II) binding to rabbit glyceraldehyde‐3‐phosphate dehydrogenase
Author(s) -
Hershberger Martin V.,
Maki August H.
Publication year - 1980
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1980.360190709
Subject(s) - chemistry , phosphorescence , tryptophan , dehydrogenase , cysteine , glyceraldehyde 3 phosphate dehydrogenase , atom (system on chip) , crystallography , enzyme , fluorescence , biochemistry , amino acid , physics , quantum mechanics , computer science , embedded system
The complex of CH 3 Hg(II) with the accessible cysteines of glyceraldehyde‐3‐phosphate dehydrogenase (GAPD, EC 1.2.1.12) from rabbit muscle has been studied by phosphorescence and optically detected magnetic resonance (ODMR) spectroscopy. The wavelength dependence of the phosphorescence decay kinetics has also been measured. Comparison of CH 3 Hg(II)–GAPD with GAPD by these methods shows that a specific optically resolved tryptophan site of GAPD is perturbed by the interaction with a nearby mercury atom. The perturbation on the luminescence and ODMR properties is typical of an external heavy‐atom effect. Based on the x‐ray diffraction structure of the lobster enzyme, it is proposed that the heavy‐atom effect results from the interaction of tryptophan‐310 with CH 3 Hg(II) bound to cysteine‐281 in the rabbit muscle enzyme.