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Non-covalent binding of the heavy atom compound Au(CN)2- at the halide binding site of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10

机译:重金属化合物Au(CN)2-在自养黄单胞菌GJ10卤代烷脱卤酶卤化物结合位点的非共价结合

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摘要

The Na[Au(CN)2] heavy atom derivative contributed considerably to the successful elucidation of the crystal structure of haloalkane dehalogenase isolated from Xanthobacter autotrophicus GJ10. The gold cyanide was located in an internal cavity of the enzyme, which also contains the catalytic residues. Refinement of the dehalogenase-gold cyanide complex at 0.25 nm to an R-factor of 16.7% demonstrates that the heavy atom molecule binds non-covalently between two tryptophan residues pointing into the active site cavity. At this same site also chloride ions can be bound. Therefore, inhibition of dehalogenase activity by the Au(CN)2- presumably occurs by competition for the same binding sate as substrates.
机译:Na [Au(CN)2]重原子衍生物极大地有助于成功阐明自自养黄单胞菌GJ10分离的卤代烷脱卤酶的晶体结构。氰化金位于酶的内部空腔中,该内部空腔还包含催化残基。将脱卤酶-金氰化物络合物在0.25 nm处精制至R因子16.7%的结果表明,重原子分子以非共价方式结合在两个指向活性位点腔的色氨酸残基之间。在同一位置,氯离子也可以结合。因此,推测Au(CN)2对脱卤素酶活性的抑制是通过竞争与底物相同的结合状态而发生的。

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