Nε,Nε-Dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein–protein complex formation
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چکیده
The reductively dimethylated derivatives of horse and yeast iso1-ferricytochromes c have been prepared and characterized for use as NMR probes of the complexes formed by cytochrome c with bovine liver cytochrome b & and yeast cytochrome c peroxidase. The electrostatic properties and structures of the derivatized cytochromes are not significantly perturbed by the modifications ; neither are the electrostatics of protein–protein complex formation or rates of interprotein electron transfer. Two-dimensional "H–"$C NMR spectroscopy of the complexes formed by the derivatized cytochromes with cytochrome b & and cytochrome c peroxidase has been used to investigate the number and identity of lysine residues of cytochrome c that are
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