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• W2113102893 endingPage "1279" @default.
• W2113102893 startingPage "1269" @default.
• W2113102893 abstract "Mammalian metallothioneins are cysteine rich metal-binding proteins comprising, when fully metalated, two metal-binding domains: the α-domain binds with M4(II)S(Cys)11 stoichiometry and the β domain binds as M3(II)S(Cys)9 stoichiometry. While the fully metalated species have been widely studied, the metalation of the apoprotein is poorly understood. Key to a description of the metalation pathway(s) is the initial conformation of the apoprotein and the arrangement of the metal-coordinating cysteines prior to metalation. We report the effect of the ill-defined, globular structure of apoMT on metalation rates. In order to overcome the experimental limitations inherent in structural determinations of a fluxional protein we used a detailed analysis of the apo-α-metallothionein conformation based on the differential rate of cysteine modification with benzoquinone. The ESI mass spectral data show the presence of two distinct conformational families: one a folded conformational family at neutral pH and a second an unfolded family of conformations at low pH. The Cd(II) metalation properties of these two conformationally distinct families were studied using stopped-flow kinetics. Surprisingly, the unfolded apoprotein metalated significantly slower than the folded apoprotein, a result interpreted as being due to the longer time required to fold into the cluster structure when the fourth Cd(II) binds. These results provide the first evidence for the role of the structure of the apo-αMT in the metalation reaction pathways and show that cysteine modification coupled with ESI-MS can be used to probe structure in cysteine-rich proteins." @default.
• W2113102893 created "2016-06-24" @default.
• W2113102893 creator A5009769045 @default.
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• W2113102893 creator A5033245457 @default.
• W2113102893 creator A5080359352 @default.
• W2113102893 date "2014-11-17" @default.
• W2113102893 modified "2023-10-10" @default.
• W2113102893 title "Metalation Kinetics of the Human α-Metallothionein 1a Fragment Is Dependent on the Fluxional Structure of the apo-Protein" @default.
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• W2113102893 doi "https://doi.org/10.1002/chem.201404283" @default.
• W2113102893 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25403957" @default.
• W2113102893 hasPublicationYear "2014" @default.
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