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Author Baltzer, L. ♦ Landergren, M.
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword BASIC BIOLOGICAL SCIENCES ♦ PORPHYRINS ♦ NUCLEAR MAGNETIC RESONANCE ♦ CHEMICAL SHIFT ♦ DATA ANALYSIS ♦ EXPERIMENTAL DATA ♦ IRON 57 ♦ MEASURING INSTRUMENTS ♦ MEASURING METHODS ♦ PROTEINS ♦ CARBOXYLIC ACIDS ♦ DATA ♦ EVEN-ODD NUCLEI ♦ HETEROCYCLIC ACIDS ♦ HETEROCYCLIC COMPOUNDS ♦ INFORMATION ♦ INTERMEDIATE MASS NUCLEI ♦ IRON ISOTOPES ♦ ISOTOPES ♦ MAGNETIC RESONANCE ♦ NUCLEI ♦ NUMERICAL DATA ♦ ORGANIC ACIDS ♦ ORGANIC COMPOUNDS ♦ ORGANIC NITROGEN COMPOUNDS ♦ RESONANCE ♦ STABLE ISOTOPES ♦ Biochemistry
Abstract The discrimination of binding between carbon monoxide and oxygen in heme proteins has inspired the syntheses of porphyrins with one side hindered by, e.g., a cap, a pocket, a strap, a basket handle, or some other device for the purpose of obstructing the binding of ligands to one side of the porphyrin, but the properties of these model hemes have not led to a straight-forward explanation of the natural regulatory mechanism. In this communication, the authors report that the {sup 57}Fe NMR chemical shifts are extremely sensitive to deformation of the porphyrin geometry and that novel information about the electronic levels may be extracted from investigations of substituent effects on the chemical shift within the simple framework of the Ramsey equation. In the hybrid basket-handle porphyrins, the ruffling leads to large changes in the iron d-orbital energies that may be important in understanding ligand binding in heme proteins and models.
ISSN 00027863
Educational Use Research
Learning Resource Type Article
Publisher Date 1990-03-28
Publisher Place United States
Journal Journal of the American Chemical Society
Volume Number 112
Issue Number 7


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