Resonance Raman, Electron Paramagnetic Resonance, and Magnetic Circular Dichroism Spectroscopic Investigation of Diheme Cytochrome c Peroxidases from Nitrosomonas europaea and Shewanella oneidensis
Author:
Affiliation:
1. Department of Chemistry and Department of Biophysics, University of Michigan, Ann Arbor, Michigan 48109, United States
2. Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, United States
Funder
University of Michigan
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00732
Reference50 articles.
1. Reactive Oxygen Species Generated at Mitochondrial Complex III Stabilize Hypoxia-inducible Factor-1α during Hypoxia
2. Structure and mechanism in the bacterial dihaem cytochrome c peroxidases
3. A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states.
4. Properties and function of the two hemes in Pseudomonas cytochrome c peroxidase
5. The Structure of an Electron Transfer Complex Containing a Cytochrome c and a Peroxidase
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