ATTENTION: The software behind KU ScholarWorks is being upgraded to a new version. Starting July 15th, users will not be able to log in to the system, add items, nor make any changes until the new version is in place at the end of July. Searching for articles and opening files will continue to work while the system is being updated. If you have any questions, please contact Marianne Reed at .

Show simple item record

dc.contributor.authorKrause, Mary Elizabeth
dc.contributor.authorGlass, Amanda M.
dc.contributor.authorJackson, Timothy A.
dc.contributor.authorLaurence, Jennifer S.
dc.identifier.citationKrause, M. E., Glass, A. M., Jackson, T. A., & Laurence, J. S. (2011). MAPping the Chiral Inversion and Structural Transformation of a Metal-Tripeptide Complex having Ni-SOD Activity. Inorganic Chemistry, 50(6), 2479–2487.
dc.descriptionThis document is the Accepted Manuscript version of a Published Work that appeared in final form in the Inorganic Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
dc.description.abstractThe metal abstraction peptide (MAP) tag is a tripeptide sequence capable of abstracting a metal ion from a chelator and binding it with extremely high affinity at neutral pH. Initial studies on the nickel-bound form of the complex demonstrate that the tripeptide asparagine-cysteine-cysteine (NCC) binds metal with 2N:2S, square planar geometry and behaves as both a structural and functional mimic of Ni superoxide dismutase (Ni-SOD). Electronic absorption, circular dichroism (CD), and magnetic CD (MCD) data collected for Ni-NCC are consistent with a diamagnetic NiII center. It is apparent from the CD signal of Ni-NCC that the optical activity of the complex changes over time. Mass spectrometry data show that the mass of the complex is unchanged. Combined with the CD data, this suggests that chiral rearrangement of the complex occurs. Following incubation of the nickel-containing peptide in D2O and back-exchange into H2O, incorporation of deuterium into non-exchangeable positions is observed, indicating chiral inversion occurs at two of the alpha carbon atoms in the peptide. Control peptides were used to further characterize the chirality of the final nickel-peptide complex, and DFT calculations were performed to validate the hypothesized position of the chiral inversions. In total, these data indicate Ni-SOD activity is increased proportionally to the degree of structural change in the complex over time, as cross-correlation between the change in CD signal and change in SOD activity reveals a linear relationship.en_US
dc.publisherAmerican Chemical Societyen_US
dc.subjectChiral inversionen_US
dc.subjectMetal Abstraction Peptide (MAP)en_US
dc.subjectD-amino aciden_US
dc.subjectSquare planaren_US
dc.subjectPeptide-metal complexen_US
dc.subjectSuperoxide dismutaseen_US
dc.titleMAPping the Chiral Inversion and Structural Transformation of a Metal-Tripeptide Complex having Ni-SOD Activityen_US
kusw.kuauthorKrause, Mary E.
kusw.kuauthorGlass, Amanda M.
kusw.kuauthorJackson, Timothy A.
kusw.kuauthorLaurence, Jennifer S.
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US

Files in this item


This item appears in the following Collection(s)

Show simple item record