M$ouml$ssbauer spectroscopy of protohaem and mesohaem cytochrome c peroxidases and their fluorides
Author:
Publisher
IOP Publishing
Subject
General Physics and Astronomy,General Engineering,Condensed Matter Physics
Link
http://stacks.iop.org/0022-3719/2/i=12/a=308/pdf
Reference23 articles.
1. Paramagnetic Resonance in some Complex Cyanides of the Iron Group II. Theory
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3. Binding in Hæmoglobin Azide as Determined by Electron Resonance: Theory of Electron Resonance in Ferrihæmoglobin Azide
4. A thermal equilibrium between high- and low-spin states in ferric cytochrome c peroxidase and some discussion on the enzyme substrate complex
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1. Role of the Heme Active Site and Protein Environment in Structure, Spectra, and Function of the Cytochrome P450s;Chemical Reviews;2000-02-01
2. Characterization of a Resting State Model of Peroxidases by ab Initio Methods: Optimized Geometries, Electronic Structures, and Relative Energies of the Sextet, Quartet, and Doublet Spin States;Journal of the American Chemical Society;1997-10-01
3. Spin-Lattice Relaxation Enhancement of Water Protons by Ferric Porphyrins Complexed with Cyclodextrins and Fluoride Ions;The Journal of Physical Chemistry;1995-05
4. Temperature dependence of the spinS=1/2 fluctuation rate and the low-spin versus high-spin transition in native chloroperoxidase;Hyperfine Interactions;1994-12
5. A Mössbauer study on an iron porphyrin model of ferric hemoproteins;Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms;1993-04
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