Properties of Human Hemoglobins with Increased Polarity in the α- or β-Heme Pocket
Open Access
- 1 September 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (37) , 23740-23749
- https://doi.org/10.1074/jbc.273.37.23740
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Crystallographic, Molecular Modeling, and Biophysical Characterization of the Valineβ67 (E11) → Threonine Variant of Hemoglobin,Biochemistry, 1996
- Mechanisms of Ligand Recognition in MyoglobinChemical Reviews, 1994
- Structural Determinants of the Stretching Frequency of CO Bound to MyoglobinBiochemistry, 1994
- Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by x-ray crystallography and infrared spectroscopyBiochemistry, 1993
- High-Resolution Crystal Structures of Distal Histidine Mutants of Sperm Whale MyoglobinJournal of Molecular Biology, 1993
- Mechanisms Regulating the Reactions of Human Hemoglobin With Oxygen and Carbon MonoxideAnnual Review of Physiology, 1990
- Alteration of sperm whale myoglobin heme axial ligation by site-directed mutagenesisBiochemistry, 1990
- Infrared spectra of carbonyl hemoglobins: characterization of dynamic heme pocket conformersBiochemistry, 1990
- Phosphocholine binding immunoglobulin Fab McPC603Journal of Molecular Biology, 1986
- Direct measurement of carbon monoxide bound to different subunits of hemoglobin A in solution and in red cells by infrared spectroscopyBiochemical and Biophysical Research Communications, 1983