2026-09-21T09:21:09Zhttps://dspace.mit.edu/server/oai/requestoai:dspace.mit.edu:1721.1/287062022-01-13T07:54:21Zcom_1721.1_7582com_1721.1_7581col_1721.1_131023
Stephen J. Lippard.
Chatwood, Lisa L., 1979-
Massachusetts Institute of Technology. Dept. of Chemistry.
Massachusetts Institute of Technology. Department of Chemistry
2005-09-27T17:53:31Z
2005-09-27T17:53:31Z
2004
2004
http://hdl.handle.net/1721.1/28706
59133374
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.
87 p.
3220951 bytes
3230615 bytes
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Massachusetts Institute of Technology
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http://dspace.mit.edu/handle/1721.1/7582
Chemistry.
Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)
Thesis
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<Abstract>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.</Abstract>
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