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Title:Covalent Attachment of Coordinatively-Saturated Metal Complexes to Horse Cytochrome-C Lysines
Author(s):Wallin, Sten Andreas
Doctoral Committee Chair(s):Scott, R.A.
Department / Program:Chemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Chemistry, Biochemistry
Chemistry, Inorganic
Abstract:The coordinatively saturated complexes $\rm Ru\sp{II}(NH\sb3)\sb5INH\sp{2+}$ (INH = isonicotinic acid) and $\rm Ru\sp{II}bp\sb2cmbpH\sp{2+}$ (bp = 2,2$\sp\prime$-bipyridine, cmbp = 4$\sp\prime$-methyl-2,2$\sp\prime$-bipyridine-4-carboxylic acid) have been covalently attached to horse cytochrome c via a carbodiimide-promoted condensation of the pendant carboxylate of the complexes with the $\varepsilon$-amine of lysine to form an amide-bond linkage.
The reaction of the O-acylisourea (Ru$\sp{II}$(NH$\sb3)\sb5$IN/EDC) $\sp{3+}$, formed by the reaction of $\rm Ru\sp{II}(NH\sb3)\sb5IN\sp{+} (pK\sb{a}$ = 2.75 $\pm$ 0.10) with EDC (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide) at pH $\sim$ 2.7, with cytochrome c at 6.0 $$ 1 s$\sp{-1}$ for the intramolecular conversion of ${\rm Ru\sp{III}}$-${\rm Fe\sp{II}}$ to ${\rm Ru\sp{III}}$-${\rm Fe\sp{III}}$.
Singly-modified Rubp$\sb2$cmbp/cyt c was prepared from (Rubp$\sb2$-cmbp/EDC) $\sp{3+}$ and cytochrome c by the same procedure used for Ru(NH$\sb3)\sb5$IN/cyt c. Preliminary peptide mapping results identify the site of modification of some of the components in the mixture of Rubp$\sb2$cmpb/cyts c. It appears that the product distribution is governed more by hydrophobic interactions between (Rubp$\sb2$cmbp/-EDC) $\sp{3+}$ and cytochrome c than by simple electrostatic considerations.
Issue Date:1988
Description:140 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1988.
Other Identifier(s):(UMI)AAI8815436
Date Available in IDEALS:2014-12-15
Date Deposited:1988

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