Probing Heme Active Sites of Hemoglobin in Functional Red Blood Cells Using Resonance Raman Spectroscopy
Author:
Affiliation:
1. Chemistry Department, Saint Louis University, 3501 Laclede Avenue, Saint Louis 63103, Missouri, United States
2. Jagiellonian Centre for Experimental Therapeutics (JCET), Jagiellonian University, 14 Bobrzyńskiego Str., Krakow 30-348, Poland
Funder
Narodowe Centrum Nauki
Saint Louis University
Narodowe Centrum Badan i Rozwoju
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.1c01199
Reference51 articles.
1. Resonance Raman Scattering Studies of the Quaternary Structure Transition in Hemoglobin
2. Ferrihemoprotein Hydroxides: A Correlation Between Magnetic and Spectroscopic Properties
3. Resonance Raman examination of axial ligand bonding and spin-state equilibriums in metmyoglobin hydroxide and other heme derivatives
4. Resonance Raman spectra of heme proteins. Effects of oxidation and spin state
5. Resonance Raman studies of methemoglobin derivatives at room temperature and 77 K
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