Resonance Raman spectroscopy and cryoenzymology have been combined to study the structures of intermediates in the peroxidase and oxidase pathways of HRP. The intermediates compound I, II, and III, have been stabilized at subzero temperatures in buffered methanol solutions. Vibrational spectra of the heme group of compounds II and III have been obtained by excitation in the vicinity of the B and Q transitions of the heme. The resultant spectra contain bands whose frequencies reveal the structure and coordination properties of the heme group in each catalytic intermediate. A comparison of these results with those for Mb, particularly between oxy-Mb and Compound III, reveal substantial differences in the low frequency regions (200 to 800 cm('-1)) and small differences in the high frequency skeletal modes. / Comparing these differences to model compounds, especially the isotopically sensitive Fe-O(,2) mode at 570 cm('-1) in Mb and 559 cm('-1) in compound III, demonstrates that the functional differences between these two proteins lies in the disposition of the proximal imidazole relative to the heme plane. / Source: Dissertation Abstracts International, Volume: 45-11, Section: B, page: 3522. / Thesis (Ph.D.)--The Florida State University, 1984.
| Identifer | oai:union.ndltd.org:fsu.edu/oai:fsu.digital.flvc.org:fsu_75465 |
| Contributors | ZIMMER, JOHN RAYMOND., Florida State University |
| Source Sets | Florida State University |
| Detected Language | English |
| Type | Text |
| Format | 329 p. |
| Rights | On campus use only. |
| Relation | Dissertation Abstracts International |
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