Reactivity of ferrous myoglobin at low pH.
Open Access
- 1 November 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (21) , 7447-7448
- https://doi.org/10.1016/s0021-9258(17)40986-0
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Binding of Carbon Monoxide to Hemoglobin Zurich. Proposal for a Kinetic ModelEuropean Journal of Biochemistry, 1977
- Dual pathways of heme protein model compound reactions with carbon monoxideJournal of the American Chemical Society, 1976
- Coordination of myoglobin active site models in aqueous solution as studied by kinetic methodsJournal of the American Chemical Society, 1975
- Ferrous porphyrins in organic solvents. II. Optical spectra and paramagnetic susceptibilitiesBiochemistry, 1974
- Functional Properties of Native and Reconstituted Hemoglobins from Chironomus thummi thummiEuropean Journal of Biochemistry, 1972
- Effects of pH on the rate of acid denaturation of horse oxy-, deoxy-, and other ferrohemoglobinsBiochemistry, 1971
- Acid denaturation of carbonylhemoglobin. Protein unfolding without heme detachmentBiochemistry, 1970
- Rates of reaction with ligands of haemoproteins reconstituted with unnatural haemsJournal of Molecular Biology, 1969