Characterization of a Resting State Model of Peroxidases by ab Initio Methods: Optimized Geometries, Electronic Structures, and Relative Energies of the Sextet, Quartet, and Doublet Spin States-Reference-Cited by-同舟云学术

Characterization of a Resting State Model of Peroxidases by ab Initio Methods: Optimized Geometries, Electronic Structures, and Relative Energies of the Sextet, Quartet, and Doublet Spin States

Published:1997-10-01 Issue:41 Volume:119 Page:9848-9851
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Loew Gilda¹,Dupuis Michel¹

Affiliation:

1. Contribution from the Molecular Research Institute, Palo Alto, California 94304, and IBM Corporation, Poughkeepsie, New York

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9715814

Reference35 articles.

1. Optical and magnetic measurements of horseradish peroxidase II. pH dependence of peroxidase

2. Magnetic Susceptibility Measurements of Cytochrome c Peroxidase and Its Complexes

3. Magnetic susceptibility measurements on hemoproteins down to 4.2°K

4. Moessbauer spectroscopic evidence for the electronic configuration of iron in horseradish peroxidase and its peroxide derivatives

5. M$ouml$ssbauer spectroscopy of protohaem and mesohaem cytochrome c peroxidases and their fluorides

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