Direct Measurement of the Nanomechanical Stability of a Redox Protein Active Site and Its Dependence upon Metal Binding.
作者： Marina I. Giannotti , Israel Cabeza de Vaca , Juan M. Artés , Fausto Sanz , Victor Guallar
关键词: Protein structure 、 Biophysics 、 Force spectroscopy 、 Crystallography 、 Chemistry 、 Plasma protein binding 、 Redox 、 Electron transfer 、 Copper 、 Azurin 、 Active site
摘要: The structural basis of the low reorganization energy cupredoxins has long been debated. These proteins reconcile a conformationally heterogeneous and exposed metal-chelating site with highly rigid copper center required for efficient electron transfer. Here we combine single-molecule mechanical unfolding experiments statistical analysis computer simulations to show that metal-binding region apo-azurin is mechanically flexible high stability imparted by binding. pathway metal depends on pulling residue suggests partial could be facilitated physical interaction certain regions redox protein.
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