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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2004.
Bacterial multicomponent monooxygenases (BMMs) are capable of oxidizing a variety of hydrocarbon substrates at a non-heme carboxylate-bridged diiron center housed within a 200-250 kDa hydroxyase protein. Chapter 1 introduces the members of the BMM family as well as several related diiron proteins with functional relevance to BMMs. The structures of the individual components and the diiron centers are discussed in relation to their catalytic function and the tuning of the metal centers. The structure of the toluene /o-xylene monooxygenase hydroxylase (ToMOH) is presented in chapter 2. The dinuclear iron center is virtually identical to that in the methane monooxygenase hydroxylase (MMOH), yet several novel features, such as a 40 [angstrom] channel, may explain the differences in the substrate specificity between BMM subfamily members. A...
Includes bibliographical references (p. 225-238).
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