Oxygen bonding in human hemoglobin and its isolated subunits: A XANES study
- 31 July 1987
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 147 (1) , 31-38
- https://doi.org/10.1016/s0006-291x(87)80083-9
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Increase of the Fe effective charge in hemoproteins during oxygenation processBiochemical and Biophysical Research Communications, 1985
- XANES study of iron displacement in the haem of myoglobinFEBS Letters, 1984
- Structure of human oxyhaemoglobin at 2·1resolutionJournal of Molecular Biology, 1983
- An investigation by iron K‐edge spectroscopy of the oxidation state of iron in hemoglobin and its subunitsFEBS Letters, 1982
- The iron–oxygen bond in human oxyhaemoglobinNature, 1982
- Electronic structure of iron–dioxygen bond in oxy-Hb-A and its isolated oxy-α and oxy-β chainsThe Journal of Chemical Physics, 1981
- Structure and refinement of oxymyoglobin at 1·6 Å resolutionJournal of Molecular Biology, 1980
- Structural changes upon oxygenation of an iron(II)(porphyrinato)(imidazole) complexJournal of the American Chemical Society, 1978
- Structure of horse carbonmonoxyhaemoglobinJournal of Molecular Biology, 1976
- 19F-nmr studies of oxygen binding to hemoglobinBiochemical and Biophysical Research Communications, 1972