Electron Spin Echo Envelope Modulation and Extended X-ray Absorption Fine Structure Studies of Active Site Models of Oxygenated Cobalt-Substituted Hemoproteins: Correlating Electron-Nuclear Couplings and Metal−Ligand Bond Lengths-Reference-Cited by-同舟云学术

Electron Spin Echo Envelope Modulation and Extended X-ray Absorption Fine Structure Studies of Active Site Models of Oxygenated Cobalt-Substituted Hemoproteins: Correlating Electron-Nuclear Couplings and Metal−Ligand Bond Lengths

Published:1997-12-17 Issue:50 Volume:119 Page:12201-12209
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lee H. Caroline¹,Scheuring Eva¹,Peisach Jack¹,Chance Mark R.¹

Affiliation:

1. Contribution from the Department of Physiology and Biophysics, Center for Synchrotron Biosciences, and Biotechnology Resource in Pulsed EPR Spectroscopy, Albert Einstein College of Medicine of Yeshiva University, Bronx, New York 10461

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9717166

Reference73 articles.

1. Coboglobins: Oxygen-Carrying Cobalt-Reconstituted Hemoglobin and Myoglobin

2. Hydrogen bonding to the bound dioxygen in oxy cobaltous myoglobin reduces the superhyperfine coupling to the proximal histidine

3. Role of hydrogen bonding to bound dioxygen in soybean leghemoglobin

4. Electron-Nuclear Coupling to the Proximal Histidine in Oxycobalt-Substituted Distal Histidine Mutants of Human Myoglobin

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