X-ray diffraction studies of a partially liganded hemoglobin, [α(FeII-CO)β(MnII)]2
- 1 April 1986
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 188 (4) , 693-706
- https://doi.org/10.1016/s0022-2836(86)80015-8
Abstract
No abstract availableThis publication has 36 references indexed in Scilit:
- Flash photolytic studies of carbon monoxide binding to the ferrous chains of manganese,iron [Mn(II),Fe(II)] hybrid hemoglobins: kinetic mechanism for the early stages of hemoglobin ligationBiochemistry, 1984
- Carbon monoxide binding to the ferrous chains of manganese,iron [Mn,Fe(II)] hybrid hemoglobins: pH dependence of the chain affinity constants associated with specific hemoglobin ligation pathwaysBiochemistry, 1984
- The crystal structure of human deoxyhaemoglobin at 1.74 Å resolutionJournal of Molecular Biology, 1984
- Bonding of molecular oxygen to T state human haemoglobinNature, 1984
- Hemoglobin tertiary structural change on ligand binding its role in the co-operative mechanismJournal of Molecular Biology, 1983
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2·5 Å resolution: Refinement of the atomic modelJournal of Molecular Biology, 1975
- Structures of deoxy and carbonmonoxy haemoglobin Kansas in the deoxy quaternary conformationJournal of Molecular Biology, 1975
- Intermediate structure of normal human haemoglobin: Methaemoglobin in the deoxy quaternary conformationJournal of Molecular Biology, 1973
- A real-space refinement procedure for proteinsActa Crystallographica Section A, 1971