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dc.contributor.author
Egli, Christine M.
dc.contributor.author
Stravs, Michael A.
dc.contributor.author
Janssen, Elisabeth M.L.
dc.date.accessioned
2020-11-26T09:28:20Z
dc.date.available
2020-11-26T04:45:10Z
dc.date.available
2020-11-26T09:28:20Z
dc.date.issued
2020-11-17
dc.identifier.issn
0013-936X
dc.identifier.issn
1520-5851
dc.identifier.other
10.1021/acs.est.0c04696
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/453112
dc.description.abstract
Extracellular enzymes are master recyclers of organic matter, and to predict their functional lifetime, we need to understand their environmental transformation processes. In surface waters, direct and indirect photochemical transformation is a known driver of inactivation. We investigated molecular changes that occur along with inactivation in aminopeptidase, an abundant class of extracellular enzymes. We studied the inactivation kinetics and localized oxidation caused by singlet oxygen, 1O2, a major photochemically derived oxidant toward amino acids. Aminopeptidase showed second-order inactivation rate constants with 1O2 comparable to those of free amino acids. We then visualized site-specific oxidation kinetics within the three-dimensional protein and demonstrated that fastest oxidation occurred around the active site and at other reactive amino acids. However, second-order oxidation rate constants did not correlate strictly with the 1O2-accessible surface areas of those amino acids. We inspected site-specific processes by a comprehensive suspect screening for 723,288 possible transformation products. We concluded that histidine involved in zinc coordination at the active site reacted slower than what was expected by its accessibility, and we differentiated between two competing reaction pathways of 1O2 with tryptophan residues. This systematic analysis can be directly applied to other proteins and transformation reactions.
en_US
dc.language.iso
en
en_US
dc.publisher
American Chemical Society
en_US
dc.title
Inactivation and Site-specific Oxidation of Aquatic Extracellular Bacterial Leucine Aminopeptidase by Singlet Oxygen
en_US
dc.type
Journal Article
dc.date.published
2020-11-04
ethz.journal.title
Environmental Science & Technology
ethz.journal.volume
54
en_US
ethz.journal.issue
22
en_US
ethz.journal.abbreviated
Environ. Sci. Technol.
ethz.pages.start
14403
en_US
ethz.pages.end
14412
en_US
ethz.grant
Environmental photochemistry of amino acid-based biomolecules
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Washington, DC
en_US
ethz.publication.status
published
en_US
ethz.grant.agreementno
159809
ethz.grant.agreementno
159809
ethz.grant.agreementno
159809
ethz.grant.fundername
SNF
ethz.grant.fundername
SNF
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
Projekte MINT
ethz.date.deposited
2020-11-26T04:45:39Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Metadata only
en_US
ethz.rosetta.installDate
2020-11-26T09:28:31Z
ethz.rosetta.lastUpdated
2022-03-29T04:06:23Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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