19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin-Reference-Cited by-同舟云学术

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19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin

Published:2000-08 Issue:4 Volume:5 Page:455-462
ISSN:0949-8257
Container-title:JBIC Journal of Biological Inorganic Chemistry
language:en
Short-container-title:J Biol Inorg Chem

Author:

Yamamoto Y.,Hirai Yueki,Suzuki Akihiro

Publisher

Springer Science and Business Media LLC

Subject

Inorganic Chemistry,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s007750050005.pdf

Cited by 17 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Spectroscopic studies of water-soluble superstructured iron(III) porphyrin. Interaction with the bovine serum albumin protein;Journal of Coordination Chemistry;2018-02-15

2. Characterization of Heme Orientational Disorder in a Myoglobin Reconstituted with a Trifluoromethyl-Group-Substituted Heme Cofactor;Biochemistry;2017-08-16

3. Characterization of Ground State Electron Configurations of High-Spin Quintet Ferrous Heme Iron in Deoxy Myoglobin Reconstituted with Trifluoromethyl Group-Substituted Heme Cofactors;Inorganic Chemistry;2016-11-21

4. 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

5. Structural characterization of imidazole adducts of heme-DNA complexes;Journal of Porphyrins and Phthalocyanines;2014-08

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