Direct immobilization of native yeast iso-1 cytochrome C on bare gold: fast electron relay to redox enzymes and zeptomole protein-film voltammetry.
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.
Heering
Hendrik A
HA
Contribution from the Department of Biotechnology, Faculty of Applied Sciences, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands.
Wiertz
Frank G M
FG
Dekker
Cees
C
de Vries
Simon
S
D002384:Catalysis; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism; D004563:Electrochemistry; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D006046:Gold / Q000737:chemistry*; D007700:Kinetics; D018625:Microscopy, Atomic Force; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D019265:Spectroscopy, Near-Infrared
C014059:CYC1 protein, S cerevisiae; D004800:Enzymes, Immobilized; D029701:Saccharomyces cerevisiae Proteins; D006046:Gold; D045304:Cytochromes c