Ligand binding to heme proteins: III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin
- 1 December 1993
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 65 (6) , 2447-2454
- https://doi.org/10.1016/s0006-3495(93)81310-9
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Resonance Raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacementBiochemistry, 1989
- Myoglobin and haemoglobin: role of distal residues in reactions with haem ligandsTrends in Biochemical Sciences, 1989
- DISCRIMINATION BETWEEN OXYGEN AND CARBON-MONOXIDE AND INHIBITION OF AUTOOXIDATION BY MYOGLOBIN - SITE-DIRECTED MUTAGENESIS OF THE DISTAL HISTIDINE1989
- The role of the distal histidine in myoglobin and haemoglobinNature, 1988
- Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine.Proceedings of the National Academy of Sciences, 1988
- Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin.Proceedings of the National Academy of Sciences, 1988
- Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy.Proceedings of the National Academy of Sciences, 1988
- 5 K extended x-ray absorption fine structure and 40 K 10-s resolved extended x-ray absorption fine structure studies of photolyzed carboxymyoglobinBiochemistry, 1987
- Kinetic, structural, and spectroscopic indentification of geminate states of myoglobin: a ligand binding site on the reaction pathwayBiochemistry, 1987
- Two types of conformers with distinct Fe-C-O configuration in the ferrous CO complex of horseradish peroxidase. Resonance Raman and infarared spectroscopic studies with native and deuteroheme-substituted enzymes.Journal of Biological Chemistry, 1987