Conformational states of hemoproteins by XANES: The mutant VR myoglobin
- 1 March 1995
- journal article
- Published by Elsevier in Physica B: Condensed Matter
- Vol. 208-209, 743-745
- https://doi.org/10.1016/0921-4526(94)01020-2
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- Intermediate states in ligand photodissociation of carboxymyoglobin studied by dispersive X-ray absorptionEuropean Biophysics Journal, 1994
- An x-ray absorption near edge structure spectroscopy study of metal coordination in Co(II)-substituted Carcinus maenas hemocyaninBiophysical Journal, 1993
- Structural and functional characterization of sperm whale myoglobin mutants: Role of arginine (E10) in ligand stabilizationBiochemistry, 1993
- Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 Å resolutionFEBS Letters, 1993
- Control and recognition of anionic ligands in myoglobinFEBS Letters, 1991
- X-ray absorption spectral study of ferric high-spin hemoproteins: XANES evidences for coordination structure of the heme ironJournal of the American Chemical Society, 1990
- Conformational Substates in ProteinsAnnual Review of Biophysics, 1988
- Low temperature X-ray investigation of structural distributions in myoglobinEuropean Biophysics Journal, 1987
- The CO bond angle of carboxymyoglobin determined by angular-resolved XANES spectroscopyNature, 1985