. This book is suitable for those who have studied the Business 2.0 B2 as an upper-intermediate course in the previous years. Hence, it can be used as a revision book as well as a reference book.
Author(s): Hanh Mai. The Business 2.0 B2 Upper Intermediate Student's Book - Free ebook download as PDF File (.pdf) or read book online for free.
This paper is designed to test your knowledge and understanding of the Business 2.0 B2 Upper Intermediate course. You must be aware of the content of the Business 2.0 B2 course as well as be able to apply the knowledge and skills learned throughout the course.
Oxford University Press 2008.This book is suitable for those who have studied the Business 2.0 B2 as an upper-intermediate course in the previous years. Hence, it can be used as a revision book as well as a reference book. The Business 2.0 B2 Upper Intermediate Student's Book.Simulation of the coordination environment of cytochrome P450cam as a function of the redox potential of the protein.
The chemical environment of the iron and copper ions of cytochrome P450cam (CYP101A1), a dioxygenase from Pseudomonas putida, is described in relation to the redox potential of the enzyme and the electrochemical midpoint potential (E(m)') of the native and oxidized forms of the protein. We have developed a molecular model of the CYP101A1 active site to compute the electrochemical potential at the protein surface. Our approach consists of building an ensemble of CYP101A1 structures, describing the flexibility of the protein backbone and the effects of the mutations to the electronic structure of the active site, and optimizing the relative electrostatic potential at the protein surface. To illustrate the effects of the mutations on the electronic structure, we have computed the DFT redox potentials of the native and oxidized CYP101A1 from the electrochemical midpoint potential (E(m)'). We have compared the computed potentials with the reported experimental potentials and found that the computed values are more consistent with the experimental data for the oxidized protein. Our molecular model describes the coordination environment of the active site metal ions as a function of the redox potential of the enzyme. This potential is controlled by the electrochemical potential at the protein surface and the electron hopping in the protein. The iron atoms are better described by a potential be359ba680
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