Movement of Fe with respect to the heme plane in the R-T transition of carp hemoglobin. An extended x-ray absorption fine structure study.
Open Access
- 1 May 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (13), 5689-5692
- https://doi.org/10.1016/s0021-9258(17)38435-1
Abstract
No abstract availableThis publication has 43 references indexed in Scilit:
- Structure and kinetics of the photoproduct of carbonylmyoglobin at low temperatures; an x-ray absorption studyBiochemistry, 1983
- Structure and refinement of oxymyoglobin at 1·6 Å resolutionJournal of Molecular Biology, 1980
- The structure of human carbonmonoxy haemoglobin at 2.7 Å resolutionJournal of Molecular Biology, 1980
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- 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
- Structure and function of haemoglobinJournal of Molecular Biology, 1967
- The Stereochemistry of the Coordination Group in an Iron(III) Derivative of TetraphenylporphineJournal of the American Chemical Society, 1967