Proton hyperfine resonance assignments in trimethylphosphine ligated ferrimyoglobin using saturation transfer spectroscopy
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference26 articles.
1. 31P chemical shifts as structural probes for heme environments. 31P-NMR study of the binding of trimethyl phosphine to various hemoglobins and myoglobins
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3. Direct observation of intermediate ligation states of hemoglobin
4. Double Nuclear Magnetic Resonance Observation of Electron Exchange between Ferri- and Ferrocytochrome c
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1. Mono- and bis-phosphine-ligated H93G myoglobin: Spectral models for ferrous-phosphine and ferrous-CO cytochrome P450;Journal of Inorganic Biochemistry;2013-10
2. Mechanism of Electron Transfer in Heme Proteins and Models: The NMR Approach;Chemical Reviews;2005-05-13
3. Phosphines as structural and functional probes of hemoproteins;Coordination Chemistry Reviews;1997-10
4. 1H NMR studies of pyridine binding to metmyoglobin;Inorganica Chimica Acta;1996-08
5. Nuclear magnetic resonance of paramagnetic metalloproteins;Chemical Reviews;1993-12
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