31P chemical shifts as structural probes for heme environments. 31P-NMR study of the binding of trimethyl phosphine to various hemoglobins and myoglobins-Reference-Cited by-同舟云学术

31P chemical shifts as structural probes for heme environments. 31P-NMR study of the binding of trimethyl phosphine to various hemoglobins and myoglobins

Published:1986-07 Issue:1-2 Volume:872 Page:163-166
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Bondon A.,Petrinko P.,Sodano P.,Simonneaux G.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference20 articles.

1. Carbon-13-iron-57 spin coupling as a new structural probe on hemoproteins. Carbon-13 nmr spectrum of iron-57-enriched carbonyl myoglobin

2. Carbon-13 magnetic resonance studies of the binding of carbon monoxide to various hemoglobins

3. Magnetic resonance studies of the binding of 13C-labeled carbon monoxide to myoglobins and hemoglobins containing modified hemes

4. Spectroscopic studies of the nature of ligand bonding in carbonmonoxyhemoglobins: evidence of a specific function for histidine-E7 from infrared and nuclear magnetic resonance intensities

5. Mechanism of T1 relaxation in 13CO complexed to an iron porphyrin: implications for CO bonding in heme proteins

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3. Mono- and bis-phosphine-ligated H93G myoglobin: Spectral models for ferrous-phosphine and ferrous-CO cytochrome P450;Journal of Inorganic Biochemistry;2013-10

4. Primary and Secondary Phosphine Complexes of Iron Porphyrins and Ruthenium Phthalocyanine: Synthesis, Structure, and P−H Bond Functionalization;Inorganic Chemistry;2008-09-19

5. Mechanism of Electron Transfer in Heme Proteins and Models: The NMR Approach;Chemical Reviews;2005-05-13