Direct Immobilization Of Native Yeast Iso-1 Cytochrome C On Bare Gold: Fast Electron Relay To Redox Enzymes And Zeptomole Protein-film Voltammetry.
Hendrik A. Heering, Frank G. M. Wiertz, Cees Dekker, Simon de Vries
Published 2004 · Chemistry, Medicine
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Cyclic voltammetry shows that yeast iso-1-cytochrome c (YCC), chemisorbed on a bare gold electrode via Cys102, exhibits fast, reversible interfacial electron transfer (k(0) = 1.8 x 10(3) s(-1)) and retains its native functionality. Vectorially immobilized YCC relays electrons to yeast cytochrome c peroxidase, and to both cytochrome cd(1) nitrite reductase (NIR) and nitric oxide reductase from Paracoccus denitrificans, thereby revealing the mechanistic properties of these enzymes. On a microelectrode, we measured nitrite turnover by approximately 80 zmol (49 000 molecules) of NIR, coadsorbed on 0.65 amol (390 000 molecules) of YCC.
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