Enzyme Modification and Oxidative Crosslinking using Carboxylate-, Phenol-and Catechol-Conjugated 1,8-Naphthalimides

Simple item page
dc.contributor.authorSova, Stacey
dc.contributor.authorKelly, Lisa A.
dc.date.accessioned2019-05-03T17:42:15Z
dc.date.available2019-05-03T17:42:15Z
dc.date.issued2019-04-16
dc.description.abstractThe ground‐ and excited‐state interactions of β‐alanine, tyrosine and L‐dopa substituted 1,8 naphthalimides (NI‐Ala, NI‐Tyr and NI‐Dopa) with lysozyme and mushroom tyrosinase were evaluated to understand the mechanism of oxidative modification. Photooxidative crosslinking of lysozyme was observed for all three conjugates. The yield was significantly reduced for NI‐Tyr and NI‐Dopa due to intramolecular electron transfer to the excited singlet state of the 1,8‐naphthalimide. Incubation of NI‐Tyr and NI‐Dopa with mushroom tyrosinase resulted in an increased fluorescence from the naphthalimide, suggesting that the phenol and catechol portion of the conjugates are oxidized by the enzyme. This results demonstrates that the compounds bind in the active site of mushroom tyrosinase. The catalytic activity of mushroom tyrosinase to oxidize both tyrosine (monophenolase) and L‐dopa (diphenolase) was modified by NI‐Tyr and NI‐Dopa. Monophenolase activity was inhibited and the diphenolase activity was enhanced in the presence of these conjugates. Detailed Michaelis‐Menten studies show that both Vmax and Km are modified, consistent with a mixed inhibition mechanism. Collectively, the results show that the compounds interact in the enzyme's active site, but also modify the distribution of the enzyme's oxidation states that are responsible for catalysis.en_US
dc.description.urihttps://onlinelibrary.wiley.com/doi/epdf/10.1111/php.13110en_US
dc.format.extent41 pagesen_US
dc.genrejournal article post-printsen_US
dc.identifierdoi:10.13016/m2yvo4-5wi2
dc.identifier.citationStacey Sova , Lisa A. Kelly , Enzyme Modification and Oxidative Crosslinking using Carboxylate‐, Phenol‐and Catechol‐Conjugated 1,8‐Naphthalimides, Photochemistry and photobiology, https://doi.org/10.1111/php.13110en_US
dc.identifier.urihttps://doi.org/10.1111/php.13110
dc.identifier.urihttp://hdl.handle.net/11603/13560
dc.language.isoen_USen_US
dc.publisherJohn Wiley & Sonsen_US
dc.relation.isAvailableAtThe University of Maryland, Baltimore County (UMBC)
dc.relation.ispartofUMBC Chemistry & Biochemistry Department Collection
dc.relation.ispartofUMBC Faculty Collection
dc.relation.ispartofUMBC Student Collection
dc.rightsThis item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
dc.rightsThis is the peer reviewed version of the following article: Stacey Sova , Lisa A. Kelly , Enzyme Modification and Oxidative Crosslinking using Carboxylate‐, Phenol‐and Catechol‐Conjugated 1,8‐Naphthalimides, Photochemistry and photobiology, https://doi.org/10.1111/php.13110, which has been published in final form at https://doi.org/10.1111/php.13110. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
dc.rightsAccess to this item will begin on April 16, 2020
dc.subjectβ‐alanine, tyrosine and L‐dopa substituted 1,8 naphthalimides (NI‐Ala, NI‐Tyr and NI‐Dopa)en_US
dc.subjecttyrosine (monophenolase)en_US
dc.subjectL‐dopa (diphenolase)en_US
dc.titleEnzyme Modification and Oxidative Crosslinking using Carboxylate-, Phenol-and Catechol-Conjugated 1,8-Naphthalimidesen_US
dc.typeTexten_US

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Sova_et_al-2019-Photochemistry_and_Photobiology.pdf
Size:
1.14 MB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
2.56 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

UMBC Chemistry & Biochemistry Department
UMBC Faculty Collection
UMBC Student Collection