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Active site specifically reconstituted nickel ii horse liver alcohol dehydrogenase ec 1.1.1.1 optical spectra of binary and ternary complexes with coenzymes coenzyme analogs substrates and inhibitors


Active site specifically reconstituted nickel ii horse liver alcohol dehydrogenase ec 1.1.1.1 optical spectra of binary and ternary complexes with coenzymes coenzyme analogs substrates and inhibitors



Journal of Inorganic Biochemistry 14(4): 297-312



ISSN/ISBN: 0162-0134

Insertion of Ni2+ into the empty catalytic site of horse liver alcohol dehydrogenase yields on active enzyme with 65% metal substitution and about 12% intrinsic activity. The electronic absorption spectrum is characterized by bands at 357 nm (2900 M-1 cm-1), 407 nm (3500 M-1 cm-1), 505 nm (300 M-1 cm-1), 570 nm (.simeq. 130 M-1 cm-1) and 680 nm (.simeq. 80 M-1 cm-1). The absorption and CD [circular dichroism] spectra are similar to those of nickel(II) azurin and nickel(II) aspartate transcarbamoylase and prove coordination of the Ni2+ to S in a distorted tetrahedral coordination geometry. Changes of the spectra upon ligand binding at the metal or conformation changes of the protein induced by coenzyme, or both, indicate alterations of the metal geometry. The chromophoric substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde forms a ternary complex with Ni2+ liver alcohol dehydrogenase and the coenzyme analogue 1,4,5,6-tetrahydroNAD, stable between pH 6 and 10. The corresponding ternary complex with NADH is only stable at pH > 9.0. The spectral redshifts induced in the substrate are 11 nm larger than those found in the zinc enzyme. Direct coordination of the substrate to the catalytic metal ion which acts as a Lewis acid in both substrate coordination and catalysis is suggested.

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Related references

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