Dw. Urry et al., ELECTROCHEMICAL TRANSDUCTION IN ELASTIC PROTEIN-BASED POLYMERS - A MODEL FOR AN ENERGY-CONVERSION STEP OF OXIDATIVE-PHOSPHORYLATION, Biochemical and biophysical research communications, 210(3), 1995, pp. 1031-1039
A pair of functional moieties, the carboxyl of an aspartic acid (Asp,
D) residue and an N-methyl nicotinamide (NMeN) formed on amide linkage
to the epsilon(-)amino group of the lysine (Lys, K) residue, are coup
led to perform energy conversion by means of controlling the transitio
n temperature, T-t, of a common hydrophobic folding and assembly domai
n within the polytricosapeptide, poly[GDGFP GVGVP GVGVP GFGVP GVGVP GV
GK{NMeN}P]. The input of electrochemical energy in the form of the red
uction of nicotinamide results in a reduction-induced increase in pKa
by 2.5 pH units which represents the performance of the chemical work
of picking up a proton. The primary structure and the structures of th
e oxidized and reduced states are verified by two-dimensional nuclear
magnetic resonance. Thus electrochemical transduction, the conversion
of electro-chemical energy into chemical energy, has been demonstrated
for the first time in a designed, synthetic protein-based polymer. (C
) 1995 Academic Press,Inc.