1H-NMR assignments and the dynamics of interconversion of the isomeric forms of cytochrome b5 in solution
- 30 November 1986
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 874 (3), 274-284
- https://doi.org/10.1016/0167-4838(86)90026-9
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Ferricytochrome b5: assignment of heme propionate resonances on the basis of nuclear Overhauser effect measurements and the nature of interprotein contacts with partner redox proteinsJournal of the American Chemical Society, 1986
- Characterization of heme orientational disorder in myoglobin by proton nuclear Overhauser effectsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: evidence for intramolecular reorientation about a heme two-fold axisJournal of the American Chemical Society, 1984
- Catalysis of Methemoglobin ReductionCurrent Topics in Cellular Regulation, 1984
- Heme orientational disorder in reconstituted and native sperm whale myoglobinJournal of Molecular Biology, 1983
- Demonstration that bovine erythrocyte cytochrome b5 is the hydrophilic segment of liver microsomal cytochrome b5Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- The orientation of the heme group in crystalline cytochrome b5Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- Structural study of the heme crevice in cytochrome based on individual assignments of the 1H-NMR lines of the heme group and selected amino acid residuesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- Contact-shifted resonances in the 1H NMR spectra of cytochrome b5 Resonance identification and spin density distribution in the heme groupBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Cytochrome b5 from a Normal Human LiverPublished by Elsevier ,1972