Skip to Main Content
Frequently Asked Questions
Submit an ETD
Global Search Box
Need Help?
Keyword Search
Participating Institutions
Advanced Search
School Logo
Files
File List
bgsu1126290895.pdf (2.34 MB)
ETD Abstract Container
Abstract Header
METAL-BINDING PROPERTIES OF SYNTHETIC METALLOPROTEINS
Author Info
Kharenko, Olesya A.
Permalink:
http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1126290895
Abstract Details
Year and Degree
2005, Doctor of Philosophy (Ph.D.), Bowling Green State University, Photochemical Sciences.
Abstract
This dissertation describes the metal-binding properties of synthetic self-assembled metalloproteins. A family of the synthetic metalloproteins was prepared based on the de novo designed peptide C16C19-GGY having the sequence Ac-K(IEALEGK)2(CEACEGK)(IEALEGK)GGY-amide. This sequence is based on the IEALEKG heptad repeat known to form two-stranded á-helical coiled coils, but was modified to contain the Cys-X-X-Cys thiolato metal binding motif found in a variety natural of metalloproteins. This cysteine-containing random coil apopeptide is capable of binding a variety of soft metal ions such as, Cu(I), Cd(II), Ag(I), Hg(II), Au(I), and Pt(II) which results in the formation of a metal-bridged self-organized á-helical bundles. It has been shown that such binding produces metal-specific oligomerization states of the resulting metalloproteins: synthetic Cu(I), Ag(I), Au(I), and Pt(II)-metalloproteins have an oligomerization state which differs from the one predicted by original design. These inorganic cofactors not only induce peptide self-assembly, but direct and transform the oligomerization state of the peptide. This illustrates how the structures of metalloproteins may be controlled by the coordination chemistry of their inorganic cofactors. A 1:1 metal:peptide stoichiometry is observed for the Cu(I) and Ag(I) adducts but the Cd(II) and Hg(II) complexes show a metal:peptide stoichiometry of 1:2. It is also shown that the Cu(I)-metalloprotein described here displays an intense room temperature long-lived (microsecond) luminescence at 600 nm. Such incorporated chemical functionality allows using this synthetic metalloprotein as a photoinduced electron-transfer agent in future studies.
Committee
Michael Ogawa (Advisor)
Pages
175 p.
Subject Headings
Chemistry, Biochemistry
Keywords
C16C19-GGY
;
METALLOPROTEINS
;
Cu
;
peptide
;
TCEP
;
¿¿¿¿M
;
METAL-BINDING
Recommended Citations
Refworks
EndNote
RIS
Mendeley
Citations
Kharenko, O. A. (2005).
METAL-BINDING PROPERTIES OF SYNTHETIC METALLOPROTEINS
[Doctoral dissertation, Bowling Green State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1126290895
APA Style (7th edition)
Kharenko, Olesya.
METAL-BINDING PROPERTIES OF SYNTHETIC METALLOPROTEINS.
2005. Bowling Green State University, Doctoral dissertation.
OhioLINK Electronic Theses and Dissertations Center
, http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1126290895.
MLA Style (8th edition)
Kharenko, Olesya. "METAL-BINDING PROPERTIES OF SYNTHETIC METALLOPROTEINS." Doctoral dissertation, Bowling Green State University, 2005. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1126290895
Chicago Manual of Style (17th edition)
Abstract Footer
Document number:
bgsu1126290895
Download Count:
1,070
Copyright Info
© 2005, all rights reserved.
This open access ETD is published by Bowling Green State University and OhioLINK.