Alteration of the proximal bond energy in the unliganded form of the homodimeric myoglobin fromNassa mutabilisKinetic and spectroscopic evidence
- 16 January 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 296 (2) , 184-186
- https://doi.org/10.1016/0014-5793(92)80375-q
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Structural Transitions Upon Ligand Binding in a Cooperative Dimeric HemoglobinScience, 1990
- Metastable intermediates in myoglobin at low pH.Proceedings of the National Academy of Sciences, 1990
- The 2.4-Å crystal structure of Scapharca dimeric hemoglobinJournal of Biological Chemistry, 1989
- Confirmation of the assignment of the iron-histidine stretching mode in myoglobinJournal of the American Chemical Society, 1984
- Amino acid sequence of dimeric myoglobin from Cerithidea rhizophorarumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Dimeric and tetrameric hemoglobins from the mollusc Scapharca inaequivalvisJournal of Molecular Biology, 1981
- Assignment of the Fe—Nϵ (His F8) stretching band in the resonance Raman spectra of deoxy myoglobinFEBS Letters, 1979
- Cooperative, Low‐Molecular‐Weight Dimeric Myoglobins from the Radular Muscle of the Gastropod Mollusc Nassa mutabilis LEuropean Journal of Biochemistry, 1977
- The amino acid sequence of a dimeric myoglobin from the gastropod mollusc, Busycon canaliculatum LFEBS Letters, 1977
- Heme-heme interactions in the oxygen equilibrium of some invertebrate myoglobinsArchives of Biochemistry and Biophysics, 1960