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Dissertation
Chiroptical and physicochemical properties of heme proteins from marine invertebrates
Doctor of Philosophy (Ph.D.), Drexel University
Jan 1990
DOI:
https://doi.org/10.17918/D8TD4H
Abstract
The respiratory proteins of many marine invertebrates are hemoglobins and myoglobins which have as their prosthetic group iron protoporphyrin IX. The hemoglobin from two species of the animal phylum Annelida and a species of the closely related phylum Echiura have been studied. Five major components of the monomeric hemoglobin from the polychaete annelid Glycera dibranchiata have been separated and characterized by absorption spectroscopy, isoelectric focusing, azide binding affinities and nitrosyl autoreduction kinetics. Similar studies have been performed on the hemoglobin from the annelid Cirriformia tentaculata and on the hemoglobin and myoglobin from the Echiuran Urechis caupo. Kinetic studies detailing the carbon monoxide driven reduction of Fe(III) proteins ere discussed in terms of distal pocket environment. In addition, oxygen binding kinetics of the hemoglobin from U. caupo are reported. Circular dichroism studies of native hemoglobins and myoglobins along with the respective apoproteins reconstituted with a synthetic symmetric porphyrin suggest that the sign and magnitude of the Soret c.d. signal are a function of both the heme orientation end surrounding globin environment.
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Details
- Title
- Chiroptical and physicochemical properties of heme proteins from marine invertebrates
- Creators
- Thomas Joseph DiFeo - DU
- Contributors
- Anthony William Addison (Advisor) - Drexel University (1970-)
- Awarding Institution
- Drexel University
- Degree Awarded
- Doctor of Philosophy (Ph.D.)
- Publisher
- Drexel University; Philadelphia, Pennsylvania
- Number of pages
- xii, 203 pages
- Resource Type
- Dissertation
- Language
- English
- Academic Unit
- College of Science (1970-1990); Drexel University
- Other Identifier
- 8166; 991014632530204721