TY - JOUR
T1 - Structural and electron transfer properties of cytochrome c adsorbed on graphite electrode studied by in situ tapping mode AFM
AU - Boussaad, S.
AU - Tao, N. J.
AU - Arechabaleta, R.
N1 - Funding Information:
Financial support is acknowledged through grants from the NIH (GM-08205) and AFSOR (F49620-96-1-0346).
PY - 1997/12/5
Y1 - 1997/12/5
N2 - We have investigated the adsorption of redox protein, cytochrome c, on graphite electrode from phosphate buffer by in situ tapping mode AFM. The protein adsorbs spontaneously onto the electrode that is covered with an adsorbed phosphate layer and forms a uniform monolayer. The adsorbed protein exhibits a reversible electron transfer at 0.17 V (Ag/AgCl) once the electrode has been increased to 0.75 V. We suggest that the adsorbed protein retains the folded conformation, and increasing the potential induces the protein to reorient its positively charged lysine residues towards the phosphate layer which promotes the electron transfer.
AB - We have investigated the adsorption of redox protein, cytochrome c, on graphite electrode from phosphate buffer by in situ tapping mode AFM. The protein adsorbs spontaneously onto the electrode that is covered with an adsorbed phosphate layer and forms a uniform monolayer. The adsorbed protein exhibits a reversible electron transfer at 0.17 V (Ag/AgCl) once the electrode has been increased to 0.75 V. We suggest that the adsorbed protein retains the folded conformation, and increasing the potential induces the protein to reorient its positively charged lysine residues towards the phosphate layer which promotes the electron transfer.
UR - http://www.scopus.com/inward/record.url?scp=0031555427&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031555427&partnerID=8YFLogxK
U2 - 10.1016/S0009-2614(97)01110-X
DO - 10.1016/S0009-2614(97)01110-X
M3 - Article
AN - SCOPUS:0031555427
SN - 0009-2614
VL - 280
SP - 397
EP - 403
JO - Chemical Physics Letters
JF - Chemical Physics Letters
IS - 3-4
ER -