The iron-proximal histidine linkage and protein control of oxygen binding in hemoglobin. A transient Raman study.
Open Access
- 1 September 1983
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 258 (17) , 10564-10572
- https://doi.org/10.1016/s0021-9258(17)44493-0
Abstract
No abstract availableThis publication has 43 references indexed in Scilit:
- Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobinJournal of Molecular Biology, 1983
- Time‐resolved resonance Raman studies of carp hemoglobinFEBS Letters, 1982
- Femtosecond photodissociation and picosecond recombination of O2 in myoglobin: A plausible explanation for the low quantum yield in MbO2Biochemical and Biophysical Research Communications, 1982
- Erythrocyte Organic Phosphates and Hemoglobin Function in Birds, Reptiles, and FishesAmerican Zoologist, 1980
- Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scatteringJournal of Molecular Biology, 1980
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- Structure of horse carbonmonoxyhaemoglobinJournal of Molecular Biology, 1976
- Correlation between quaternary structure and ligand dissociation kinetics for fully liganded hemoglobinBiochemistry, 1975
- Structure of deoxyhaemoglobin Yakima: A high-affinity mutant form exhibiting oxy-like α1β2 subunit interactionsJournal of Molecular Biology, 1973
- Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobinBiochemistry, 1973