De novo designed safranine enzymes
Item
-
Title
-
De novo designed safranine enzymes
-
Identifier
-
d_2009_2013:85cf7440d99b:11518
-
identifier
-
11993
-
Creator
-
Raju, Gheevarghese,
-
Contributor
-
Ronald L. Koder
-
Date
-
2012
-
Language
-
English
-
Publisher
-
City University of New York.
-
Subject
-
Biophysics | Biochemistry | Chemistry | Artificial Enzymes | Atherosclerosis | Biocatalytic green chemistry | Biosensor | Cancer prodrug activation | Safranines
-
Abstract
-
De novo designed safranine enzymes are functionally parallel to NAD(P)H: flavinnitroreductases. The non-natural redox cofactor safranine has a very low reduction potential, -290 mV versus flavins -190 mV. A difference of 100 mV provides an additional 2.3 Kcal/mol energy to drive reduction reactions. Also safranine has an intrinsic unstable semiquinone oxidation state providing a doorstep for hydride transfer mechanism. Hence safranine enzymes will perform the electron transfer reaction, which is similar to the natural nitroreductases avoiding all oxygen activating free-radical side reactions. We designed a whole series of safranine binding helical bundles which catalyzes NAD(P)H dependent nitroaromatic reduction. Latest studied saf-X and safX-Loop proteins hold promise towards fully functional artificial enzymes.;A novel synthesis pathway of generating different safranine derivatives was developed. These derivatives differ in their characteristic reduction potentials, fluorescent and visible spectra. This will allow the amendment of reduction reaction towards any particular nitroaromatic substrate. Our goal is to create artificial safranine enzymes, which can be used for cancer prodrug activation, treatment of atherosclerosis, explosive sensing, biofuels as well as green chemical catalysis.
-
Type
-
dissertation
-
Source
-
2009_2013.csv
-
degree
-
Ph.D.
-
Program
-
Chemistry
