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Massachusetts Institute of Technology

Structural studies of bacterial multicomponent monooxygenases : insights into substrate specificity, diiron center tuning and component interactions

Abstract

dc:description.abstract

(cont.) α-subunit cavities. The presence of 6-bromohexan-l-ol induces one of the active site helices to adopt a [pi] conformation. Together, these findings suggest modes by which molecules may move through the MMOH cavities and how both substrates and MMOB may influence the structure of the active site pocket.

Degree

thesis:*
Department dc:contributor.department
Massachusetts Institute of Technology. Department of Chemistry
Grantor dc:publisher
Massachusetts Institute of Technology
Year dc:date.issued
2004

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Sazinsky, Matthew H. (Matthew Howard), 1976-
Advisor dc:contributor.advisor
  • Stephen J. Lippard.

Subjects

dc:subject × 1

Rights

dc:rights
Statement dc:rights
  • 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.
Language dc:language.iso
en_US

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/1721.1/28702
OAI identifier oai:identifier
oai:dspace.mit.edu:1721.1/28702

Chain of custody

source
Harvested from
MIT
Base URL
dspace.mit.edu/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
related terms
citation

Sazinsky, Matthew H. (Matthew Howard), 1976-. Structural studies of bacterial multicomponent monooxygenases : insights into substrate specificity, diiron center tuning and component interactions. Massachusetts Institute of Technology, 2004. http://hdl.handle.net/1721.1/28702