Hydrogen Bonding of Tyrosine B10 to Heme-bound Oxygen in Ascaris Hemoglobin: DIRECT EVIDENCE FROM UV RESONANCE RAMAN SPECTROSCOPY
Open Access
- 12 January 1996
- journal article
- Published by Elsevier
- Vol. 271 (2), 958-962
- https://doi.org/10.1074/jbc.271.2.958
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Functional Aspects of Ultra-rapid Heme Doming in Hemoglobin, Myoglobin, and the Myoglobin Mutant H93GPublished by Elsevier ,1995
- Mechanisms of Ligand Recognition in MyoglobinChemical Reviews, 1994
- Polar zippersCurrent Biology, 1993
- Investigation of higher order structures of proteins by ultraviolet resonance Raman spectroscopyProgress in Biophysics and Molecular Biology, 1992
- Hemoglobin quaternary structure change monitored directly by transient UV resonance Raman spectroscopyJournal of the American Chemical Society, 1989
- Effect of solvent viscosity on the heme-pocket dynamics of photolyzed (carbonmonoxy)hemoglobinBiochemistry, 1988
- Tyrosine hydrogen-bonding and environmental effects in proteins probed by ultraviolet resonance Raman spectroscopyBiochemistry, 1988
- H2 Raman‐shifted YAG laser ultraviolet Raman spectrometer operating at wavelengths down to 184 nmJournal of Raman Spectroscopy, 1986
- UV resonance Raman spectroscopy of the aromatic amino acids and myoglobinJournal of the American Chemical Society, 1984
- On cytochrome, a respiratory pigment, common to animals, yeast, and higher plantsProceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character, 1925