期刊
METALLOMICS
卷 12, 期 2, 页码 273-279出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9mt00261h
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资金
- National Research Foundation of Korea [2016R1C1B2008836]
- Business for Cooperative R&D Between Industry, Academia, and Research Institute - Korea Small and Medium Business Administration [C0541528]
- Korea Technology & Information Promotion Agency for SMEs (TIPA) [C0541528] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2016R1C1B2008836] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Amicyanin is a type I copper protein that mediates electron transfer between methylamine dehydrogenase and cytochrome c-(551i) for energy production in Paracoccus denitrificans. Although the Met98 axial ligand of amicyanin has been shown to dictate metal selectivity and specificity during protein folding, the mechanism involved in copper-mediated amicyanin folding is unknown. Here, we kinetically and spectroscopically described reaction steps for incorporating copper into fully and less folded apo-amicyanin and established thermodynamic parameters for two amicyanin folding states. The rate constant for the incorporation of copper into fully folded apo-amicyanin at 25 degrees C was almost 1.5-fold lower than that for the initial phase of copper addition to the less folded apo-amicyanin. However, the rate constant was 10-fold higher than that of the second phase of copper addition to less folded apo-amicyanin at 25 degrees C. When overall binding energetic parameters (Delta H degrees and Delta S degrees) for the incorporation of copper into fully folded apo-amicyanin were measured by the van't Hoff method and isothermal titration calorimetry, the values were more positive than those determined for less folded apo-amicyanin. This indicates that during amicyanin biogenesis, copper rapidly binds to an unfolded apo-amicyanin active site, inducing protein folding and favorably influencing subsequent organization of copper ligands.
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