Raman difference spectroscopy of heme-linked ionizations in cytochrome c peroxidase.
Open Access
- 1 February 1983
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 258 (4) , 2168-2173
- https://doi.org/10.1016/s0021-9258(18)32903-x
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- Protein influences on porphyrin structure in cytochrome cBiochemistry, 1981
- Raman difference spectroscopy as a probe of biological moleculesJournal of Raman Spectroscopy, 1981
- Raman difference spectroscopy of tertiary and quaternary structure changes in methaemoglobinsNature, 1980
- Resonance raman study of the heme-linked ionization in reduced horseradish peroxidaseBiochemical and Biophysical Research Communications, 1980
- Methemoglobin imidazole: evidence against an IHP‐induced change in quaternary structureFEBS Letters, 1980
- Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogsJournal of the American Chemical Society, 1976
- Nature of the iron-ligand bond in ferrous low spin hemoproteins studied by resonance Raman scatteringJournal of the American Chemical Society, 1976
- Kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strengthBiochemistry, 1975
- Resonance Raman spectra of metallooctaethylporphyrins. Structural probe of metal displacementJournal of the American Chemical Society, 1975
- Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidaseBiochemistry, 1974