Structural and mutagenesis studies of soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)
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59133374-MIT.pdf
Description
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3.08 MB
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Checksum (MD5)
928305e65f4b7d398eece24a7ea6b398
Author(s)
Chatwood, Lisa L., 1979-
Advisor(s)
Stephen J. Lippard.
Date Issued
2004
Publisher
Massachusetts Institute of Technology
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.
Description
Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2004.
Vita.
Includes bibliographical references.
Subjects
Chemistry.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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