Infrared spectroscopic evidence of hydrogen bonding between carbon monoxide and protein in carbonylhorseradish peroxidase C
- 14 November 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 163 (2), 303-305
- https://doi.org/10.1016/0014-5793(83)80840-0
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Synthesis and oxygenation studies of monomolecular hemoprotein modelsInorganica Chimica Acta, 1983
- Infrared spectra of carbonyl lactoperoxidaseInorganica Chimica Acta, 1983
- Evidence for hydrogen bonding of bound dioxygen to the distal histidine of oxycobalt myoglobin and haemoglobinNature, 1982
- The iron–oxygen bond in human oxyhaemoglobinNature, 1982
- Kinetic evidence for dioxygen stabilization in oxygenated iron(II)-porphyrins by distal polar interactionsJournal of the Chemical Society, Chemical Communications, 1982
- Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobinNature, 1981
- LIGAND BINDING TO HEMOGLOBINS: EFFECTS OF GLOBIN STRUCTURE11This work was supported in part by U.S. Public Health Service Grants HL-15980 (W.S.C.) and HL-02799 (S.C.).Published by Elsevier ,1978
- Infrared spectroscopic studies of carbonyl horseradish peroxidasesBiochemistry, 1976
- Four Isoperoxidases from Horse Radish Root.Acta Chemica Scandinavica, 1970
- 33. Physical properties of anthraquinone and its derivatives. Part I. Infrared spectraJournal of the Chemical Society, 1959