Methods in Enzymology Vol.226 Metallobiochemistry Part C: Spectroscopic and Physical Methods for Pro

Discussion in 'Methods in Enzymology Book Series' started by nguyenhuuthien_42, Jul 29, 2016.

  1. nguyenhuuthien_42

    nguyenhuuthien_42 New Member

    We have seen from the previous discussion that absorption spectral studies in the ligand field region probe the energy splittings of thed orbitals and that this relates to the geometry of the metal center. The energies and intensities of ligand-to-metal charge transfer transitions sensitively probe bonding interactions of the ligand with the metal center. Charge transfer transitions can be used both quanlitatively to observe ligand binding to a metal center, owing to the requirement of orbital overlap for significant charge transfer intensity, and quantitatively to define the electron donor ability of that ligand and experimentally evaluate the results of electronic structure calculations. Studies of the intensities of peaks at the ligand K edge can define the covalent interaction of the ligand with the metal valence orbitals, whereas copper K-edge spectroscopy is a powerful probe of metal ion oxidation state and the ligand field geometry ofd10 cuprous sites that are inaccessible through other spectoscopic methods. Absorption spectral studies in all regions are strongly complemented by CD, variable temperature MCD, and single-crystal polarized absorption spectroscopies, which should also be pursued whenever possible to obtain detailed electronic structural insight of relevance to catalysis.
    • Series: Methods in Enzymology (Book 226)
    • Hardcover: 674 pages
    • Publisher: Academic Press;
    • Language: English
    • ISBN-10: 0121821277
    • ISBN-13: 978-0121821272
    • Product Dimensions: 1.2 x 6.5 x 9.5 inches
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    Last edited by a moderator: Feb 6, 2022

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