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• W2049202388 endingPage "3772" @default.
• W2049202388 startingPage "3761" @default.
• W2049202388 abstract "The powerful combination of 113Cd NMR and 111mCd PAC (perturbed angular correlation) spectroscopies has been critical to determine the coordination geometry of CdII bound to thiolate-rich centers. We have obtained important linear correlations between 113Cd NMR and 111mCd PAC spectroscopic data and the acid/base properties of the metal binding site that illustrate the presence of a dynamic model for metal binding (see figure). These unique results can give new insight into CdII-substituted ZnII proteins. CdII has been used as a probe of zinc metalloenzymes and proteins because of the spectroscopic silence of ZnII. One of the most commonly used spectroscopic techniques is 113Cd NMR; however, in recent years 111mCd Perturbed Angular Correlation spectroscopy (111mCd PAC) has also been shown to provide useful structural, speciation and dynamics information on CdII complexes and biomolecules. In this article, we show how the joint use of 113Cd NMR and 111mCd PAC spectroscopies can provide detailed information about the CdII environment in thiolate-rich proteins. Specifically we show that the 113Cd NMR chemical shifts observed for CdII in the designed TRI series (TRI=Ac-G(LKALEEK)4G-NH2) of peptides vary depending on the proportion of trigonal planar CdS3 and pseudotetrahedral CdS3O species present in the equilibrium mixture. PAC spectra are able to quantify these mixtures. When one compares the chemical shift range for these peptides (from δ=570 to 700 ppm), it is observed that CdS3 species have δ 675–700 ppm, CdS3O complexes fall in the range δ 570–600 ppm and mixtures of these forms fall linearly between these extremes. If one then determines the pKa2 values for CdII complexation [pKa2 is for the reaction Cd[(peptide−H)2(peptide)]+→Cd(peptide)3− + 2H+] and compares these to the observed chemical shift for the Cd(peptide)3− complexes, one finds that there is also a direct linear correlation. Thus, by determining the chemical shift value of these species, one can directly assess the metal-binding affinity of the construct. This illustrates how proteins may be able to fine tune metal-binding affinity by destabilizing one metallospecies with respect to another. More important, these studies demonstrate that one may have a broad 113Cd NMR chemical shift range for a chemical species (e.g., CdS3O) which is not necessarily a reflection of the structural diversity within such a four-coordinate species, but rather a consequence of a fast exchange equilibrium between two related species (e.g., CdS3O and CdS3). This could lead to reinterpretation of the assignments of cadmium–protein complexes and may impact the application of CdII as a probe of ZnII sites in biology." @default.
• W2049202388 created "2016-06-24" @default.
• W2049202388 creator A5030625779 @default.
• W2049202388 creator A5033340669 @default.
• W2049202388 creator A5044615615 @default.
• W2049202388 creator A5050922058 @default.
• W2049202388 creator A5084987684 @default.
• W2049202388 date "2009-02-19" @default.
• W2049202388 modified "2023-10-02" @default.
• W2049202388 title "The Correlation of¹¹³Cd NMR and^111mCd PAC Spectroscopies Provides a Powerful Approach for the Characterization of the Structure of Cd^II-Substituted Zn^IIProteins" @default.
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• W2049202388 doi "https://doi.org/10.1002/chem.200802105" @default.
• W2049202388 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3598615" @default.
• W2049202388 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19229934" @default.
• W2049202388 hasPublicationYear "2009" @default.
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