Structure of a stable form of sulfheme

A stable green heme was extracted from ferric cyanosulfmyoglobin after it had undergone an internal conversion reaction. After iron removal and conversion to the methyl ester, the resulting green porphyrin was purified by high-pressure liquid chromatography. Visible, 1H NMR, and mass spectrometric s...

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Bibliographic Details
Published in:Biochemistry (Easton) 1986-12, Vol.25 (26), p.8458-8466
Main Authors: Bondoc, Laureano L, Chau, Mei Hing, Price, Mary Ann, Timkovich, Russell
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Drug Stability
Fundamental and applied biological sciences. Psychology
Heme - analogs & derivatives
Heme - isolation & purification
Hemoproteins
Horses
Magnetic Resonance Spectroscopy - methods
Metalloproteins
Muscles
Myoglobin
Porphyrins
Proteins
Pyrroles
Spectrophotometry - methods
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Summary:A stable green heme was extracted from ferric cyanosulfmyoglobin after it had undergone an internal conversion reaction. After iron removal and conversion to the methyl ester, the resulting green porphyrin was purified by high-pressure liquid chromatography. Visible, 1H NMR, and mass spectrometric studies provided evidence to identify the substituents of the porphyrin. Nuclear Overhauser enhancements enabled an assignment of the single modified pyrrole. Substituent positions 1, 2, 5, 6, 7, and 8 have the original protoporphyrin IX substituents. At ring B, the 4-vinyl group has cyclized with a single sulfur atom to form a fifth ring with a 2,5-dihydrothiophene type of structure.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00374a021