Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)
Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2004.
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| Format: | Thesis |
| Language: | en_US |
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Massachusetts Institute of Technology
2005
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| Online Access: | http://hdl.handle.net/1721.1/28706 |
| _version_ | 1811072497654693888 |
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| author | Chatwood, Lisa L., 1979- |
| author2 | Stephen J. Lippard. |
| author_facet | Stephen J. Lippard. Chatwood, Lisa L., 1979- |
| author_sort | Chatwood, Lisa L., 1979- |
| collection | MIT |
| description | Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2004. |
| first_indexed | 2024-09-23T09:06:54Z |
| format | Thesis |
| id | mit-1721.1/28706 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T09:06:54Z |
| publishDate | 2005 |
| publisher | Massachusetts Institute of Technology |
| record_format | dspace |
| spelling | mit-1721.1/287062019-04-10T14:36:50Z Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) Chatwood, Lisa L., 1979- Stephen J. Lippard. Massachusetts Institute of Technology. Dept. of Chemistry. Massachusetts Institute of Technology. Dept. of Chemistry. Chemistry. Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2004. Vita. Includes bibliographical references. The solution structure for the 27 kDa flavin binding domain of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) was solved by NMR spectroscopy. The structure consists of a two domains, an FAD binding domain with a six-stranded antiparallel β-barrel and one α-helix, and an NADH binding domain with a five-stranded parallel β-sheet surrounded by four α-helices. The FAD cofactor is bound at the interface between the two domains in a novel conformation. Near this FAD cofactor, a conserved C-terminal phenylalanine residue is proposed to act as a conformational gate for electron transfer. Kinetic studies on a series of mutants confirm that this phenylalanine controls electron transfer by regulating access of NADH substrate to the bound flavin cofactor. by Lisa L. Chatwood. S.M. 2005-09-27T17:53:31Z 2005-09-27T17:53:31Z 2004 2004 Thesis http://hdl.handle.net/1721.1/28706 59133374 en_US M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 87 p. 3220951 bytes 3230615 bytes application/pdf application/pdf application/pdf Massachusetts Institute of Technology |
| spellingShingle | Chemistry. Chatwood, Lisa L., 1979- Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) |
| title | Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) |
| title_full | Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) |
| title_fullStr | Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) |
| title_full_unstemmed | Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) |
| title_short | Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath) |
| title_sort | structural and mutagenesis studies of soluble methane monooxygenase reductase from methylococcus capsulatus bath |
| topic | Chemistry. |
| url | http://hdl.handle.net/1721.1/28706 |
| work_keys_str_mv | AT chatwoodlisal1979 structuralandmutagenesisstudiesofsolublemethanemonooxygenasereductasefrommethylococcuscapsulatusbath |