Resonance Raman studies of acetylheme-reconstituted myoglobins. Characterization of 2- versus 4-substituent/protein interactions
- 1 December 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 26 (25) , 8319-8326
- https://doi.org/10.1021/bi00399a044
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 19 references indexed in Scilit:
- Haem disorder in reconstituted human haemoglobinBiochemical Journal, 1982
- Resonance Raman spectroscopic studies of axial ligation in oxyhemoglobin and oxymyoglobin, and nitrosylmyoglobinBiochemistry, 1982
- Studies on Reconstituted Myoglobins and Hemoglobins. I. Role of the Heme Side Chains in the Oxygenation of Myoglobin1The Journal of Biochemistry, 1982
- Structure and refinement of oxymyoglobin at 1·6 Å resolutionJournal of Molecular Biology, 1980
- Resonance Raman spectra of myoglobins reconstituted with Spirographis and Isospirographis hemes and iron 2,4-diformylprotoporphyrinBiochemistry, 1980
- Resonance Raman spectra and optical properties of oxidized cytochrome oxidaseBiochemistry, 1979
- Porphyrin-protein bond of cytochrome c558 from Euglena gracilisJournal of the American Chemical Society, 1977
- Structure of myoglobin refined at 2·0 Å resolutionJournal of Molecular Biology, 1977
- Synthesis and Moessbauer spectra of octaethylporphyrin ferrous complexesJournal of the American Chemical Society, 1976
- Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogsJournal of the American Chemical Society, 1976