Discordant Results on FeCO Deformability in Heme Proteins Reconciled by Density Functional Theory
- 28 April 1998
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (18) , 4524-4525
- https://doi.org/10.1021/ja9732946
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Crystal Structures of CO−, Deoxy- and Met-myoglobins at Various pH ValuesJournal of Molecular Biology, 1996
- The Proximal Residue Largely Determines the CO Distortion in Carbon Monoxy Globin Proteins. An ab Initio Study of a Heme Prosthetic UnitThe Journal of Physical Chemistry, 1995
- Determination of CO orientation in myoglobin by single-crystal infrared linear dichroismJournal of the American Chemical Society, 1994
- Mechanisms of Ligand Recognition in MyoglobinChemical Reviews, 1994
- Structural Determinants of the Stretching Frequency of CO Bound to MyoglobinBiochemistry, 1994
- How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and modelsJournal of the American Chemical Society, 1994
- High-Resolution Crystal Structures of Distal Histidine Mutants of Sperm Whale MyoglobinJournal of Molecular Biology, 1993
- Hydration in protein crystals. A neutron diffraction analysis of carbonmonoxymyoglobinActa crystallographica Section B, Structural science, crystal engineering and materials, 1990
- X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolutionJournal of Molecular Biology, 1986
- Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogsJournal of the American Chemical Society, 1976