19F NMR Study of the Heme Orientation and Electronic Structure in a Myoglobin Reconstituted with a Ring-Fluorinated Heme
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
https://www.jstage.jst.go.jp/article/bcsj/73/10/73_10_2309/_pdf
Reference37 articles.
1. Nmr Study Of Active Sites In Paramagnetic Haemoproteins
2. Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins.
3. Proton NMR characterization of metastable and equilibrium heme orientational heterogeneity in reconstituted and native human hemoglobin
4. Proton NMR study of the influence of hydrophobic contacts on protein prosthetic group recognition in bovine and rat ferricytochrome b5
5. Functional effects of heme orientational disorder in sperm whale myoglobin.
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1. Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin;Biochemistry;2018-09-14
2. Characterization of Heme Orientational Disorder in a Myoglobin Reconstituted with a Trifluoromethyl-Group-Substituted Heme Cofactor;Biochemistry;2017-08-16
3. Effect of the Electron Density of the Heme Fe Atom on the Fe–Histidine Coordination Bond in Deoxy Myoglobin;Bulletin of the Chemical Society of Japan;2014-08-15
4. Field-dependent 19F NMR study of sperm whale myoglobin reconstituted with a ring-fluorinated heme;Polymer Journal;2012-04-18
5. Characterization of the acid–alkaline transition in the individual subunits of human adult and foetal methaemoglobins;The Journal of Biochemistry;2010-06-02
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