Abstract
In this paper, we characterise the process of immobilisation of cytochrome c at a gold surface modified with the short chain alkyl-thiol self-assembled monolayer, mercaptopropionic acid. Using high resolution X-ray photoelectron spectroscopy, we reveal detail of the step-by-step construction of the biomolecular structure at a self-assembled monolayer, measured during two different immobilisation protocols involving either a carbodiimide activated intermediate or aminolysis of a succinimide ester by the protein. Finally, we relate the subtle variations in the charged species produced during the immobilisation procedures to differences that we measure in the protein's redox potential.
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