Inequivalent Conformational Response of Chironomus Hemoglobins to Ligation with O2 and CO.. A Circular-Dichroism and Infrared-Spectroscopic Study
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1977.tb11241.x/fullpdf
Reference28 articles.
1. Ligand-Dependent Bohr Effect of Chironomus Hemoglobins
2. Origin of the rotational strength of heme transitions of myoglobin
3. Origin of the heme Cotton effects in myoglobin and hemoglobin
4. The Influence of the Aromatic Amino Acid Side-Chains on the Sign of the Soret Cotton Effect in Chironomus Hemoglobin (CTT III)
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1. Assignment of selected hyperfine proton NMR resonances in the met forms of Glycera dibranchiata monomer hemoglobins and comparisons with sperm whale metmyoglobin;Biochemistry;1988-04-19
2. Resonance Raman investigation of CO-ligated monomeric insect hemoglobins. Direct evidence for reciprocal changes in iron-axial ligand bonds induced by allosteric transitions.;Journal of Biological Chemistry;1986-07
3. Correlations between reduction potential, carbonyl stretch frequency, and carbonyl half-band width in hemoproteins;Biochemistry;1984-12-18
4. Iron-carbon bond lengths in carbonmonoxy and cyanomet complexes of the monomeric hemoglobin III from Chironomus thummi thummi: a critical comparison between resonance Raman and x-ray diffraction studies.;Proceedings of the National Academy of Sciences;1984-08-01
5. Significant heterogeneity in the monomer fraction of Glycera dibranchiata hemoglobins. Detection, partial isolation and characterization of several protein components;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1983-01
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