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dc.contributor.advisorBaker, Gary M.en_US
dc.contributor.authorYergul, E. Serapen_US
dc.date.accessioned2016-01-29T21:23:26Z
dc.date.available2016-01-29T21:23:26Z
dc.date.issued1994
dc.identifier.urihttp://commons.lib.niu.edu/handle/10843/15138
dc.descriptionIncludes bibliographical references (pages [59]-61)en_US
dc.description.abstractThe effect of temperature on the two heme centers has been examined in cytochrome c oxidase that was solubilized in n-dodecyl (3-D-maltoside (DM). The goal of the work was to systematically find experimental conditions that resolved selective thermal effects on the two hemes. We focused on spectral changes occuring at 45°C in high DM concentration. Under these conditions, we observed isosbestic points and a new charge transfer band at 635 nm. Reduced minus oxidized spectra of cytochromes a and a3 were resolved to identify thermally induced changes in each heme. The 635 nm band was assigned to cytochrome a. Loss of the 655 nm band, due to high spin cytochrome a3 was also observed, indicating that both hemes were thermally sensitive. A binding study of formate and cyanide was also used to selectively probe cytochromes a and a3en_US
dc.format.extent61 pagesen_US
dc.language.isoengen_US
dc.publisherNorthern Illinois Universityen_US
dc.rightsNIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.en_US
dc.subject.lcshCytochrome oxidaseen_US
dc.titleUse of temperature to selectively probe the cytochrome a and a? centers of bovine heart cytochrome c oxidaseen_US
dc.type.genreDissertation/Thesisen_US
dc.typeTexten_US
dc.contributor.departmentDepartment of Chemistryen_US
dc.description.degreeM.S. (Master of Science)en_US


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