The hydrogen-bonded water network in the oxygen-evolving complex of photosystem II

dc.contributor.advisor Barry, Bridgette A.
dc.contributor.author Polander, Brandon C.
dc.contributor.committeeMember Oyelere, Adeboyega K.
dc.contributor.committeeMember Lieberman, Raquel L.
dc.contributor.committeeMember Curtis, Jennifer E.
dc.contributor.committeeMember Sherrill, David
dc.contributor.department Chemistry and Biochemistry
dc.date.accessioned 2014-01-13T16:19:35Z
dc.date.available 2014-01-13T16:19:35Z
dc.date.created 2013-12
dc.date.issued 2013-08-14
dc.date.submitted December 2013
dc.date.updated 2014-01-13T16:19:35Z
dc.description.abstract Protein dynamics play a key role in enzyme-catalyzed reactions. Vibrational spectroscopy provides a method to follow these structural changes and thereby describe the reaction coordinate as a function of space and time. A vibrational spectroscopic technique, reaction-induced FTIR spectroscopy, has been applied to the study of the oxygen-evolving complex (OEC) of photosystem II (PSII). In plant photosynthesis, PSII evolves oxygen from the substrate, water, by the accumulation of photo-oxidizing equivalents at the OEC. Molecular oxygen and protons are the products of this reaction, which is responsible for the maintenance of an aerobic atmosphere on earth. The OEC is a Mn4CaO5 cluster with nearby bound chloride ions. Sequentially oxidized states of the OEC are termed the S states. The dark-stable state is S1, and oxygen is released on the transition from S3 to S0. Using short laser flashes, individual S states are generated, allowing vibrational spectroscopy to be used to study these different oxidation states of the OEC. In current X-ray crystal structures, hydrogen bonds to water molecules are predicted to form an extensive network around the Mn4CaO5 cluster. In the OEC, four peptide carbonyl groups are linked to the water network, which extends to two Mn-bound and two Ca-bound water molecules. This dissertation discusses a vibrational spectroscopic method that uses these peptide carbonyl frequencies as reporters of solvatochromic changes in the OEC. This technique provides a new, high-resolution method with which to study water and protein dynamics in PSII and other enzymes.
dc.description.degree Ph.D.
dc.format.mimetype application/pdf
dc.identifier.uri http://hdl.handle.net/1853/50222
dc.language.iso en_US
dc.publisher Georgia Institute of Technology
dc.subject Photosystem II
dc.subject Vibrational spectroscopy
dc.subject Water oxidation
dc.subject Amide carbonyl frequency
dc.subject Reaction-induced FTIR
dc.subject.lcsh Proteins
dc.subject.lcsh Molecular dynamics
dc.subject.lcsh Photosynthesis
dc.title The hydrogen-bonded water network in the oxygen-evolving complex of photosystem II
dc.type Text
dc.type.genre Dissertation
dspace.entity.type Publication
local.contributor.advisor Barry, Bridgette A.
local.contributor.corporatename School of Chemistry and Biochemistry
local.contributor.corporatename College of Sciences
relation.isAdvisorOfPublication 3398b34c-4658-496b-84ec-43b16a2007e0
relation.isOrgUnitOfPublication f1725b93-3ab8-4c47-a4c3-3596c03d6f1e
relation.isOrgUnitOfPublication 85042be6-2d68-4e07-b384-e1f908fae48a
thesis.degree.level Doctoral
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
98.63 MB
Adobe Portable Document Format
License bundle
Now showing 1 - 2 of 2
No Thumbnail Available
3.87 KB
Plain Text
No Thumbnail Available
3.87 KB
Plain Text