PMID- 17549469
OWN - NLM
STAT- MEDLINE
DCOM- 20080325
LR  - 20181113
IS  - 0175-7571 (Print)
IS  - 0175-7571 (Linking)
VI  - 36
IP  - 8
DP  - 2007 Nov
TI  - Kinetics of the electron transfer reaction of Cytochrome c (552) adsorbed on 
      biomimetic electrode studied by time-resolved surface-enhanced resonance Raman 
      spectroscopy and electrochemistry.
PG  - 1039-48
AB  - Cytochrome c (552) (Cyt-c (552)) and its redox partner ba ( 3 )-oxidase from 
      Thermus thermophilus possess structural differences compared with Horse heart 
      cytochrome c (cyt-c)/cytochrome c oxidase (CcO) system, where the recognition 
      between partners and the electron transfer (ET) process is initiated via 
      electrostatic interactions. We demonstrated in a previous study by 
      surface-enhanced resonance Raman (SERR) spectroscopy that roughened silver 
      electrodes coated with uncharged mixed self-assembled monolayers HS-(CH(2))( n 
      )-CH(3)/HS-(CH(2))( n + 1)-OH 50/50, n = 5, 10 or 15, was a good model to mimic 
      the Cyt-c (552) redox partner. All the adsorbed molecules are well oriented on 
      such biomimetic electrodes and transfer one electron during the redox process. 
      The present work focuses on the kinetic part of the heterogeneous ET process of 
      Cyt-c (552) adsorbed onto electrodes coated with such mixed SAMs of different 
      alkyl chain length. For that purpose, two complementary methods were combined. 
      Firstly cyclic voltammetry shows that the ET between the adsorbed Cyt-c (552) and 
      the biomimetic electrode is direct and reversible. Furthermore, it allows the 
      estimation of both the density surface coverage of adsorbed Cyt-c (552) and the 
      kinetic constants values. Secondly, time-resolved SERR (TR-SERR) spectroscopy 
      showed that the ET process occurs without conformational change of the Cyt-c 
      (552) heme group and allows the determination of kinetic constants. Results show 
      that the kinetic constant values obtained by TR-SERR spectroscopy could be 
      compared to those obtained from cyclic voltammetry. They are estimated at 200, 
      150 and 40 s(-1) for the ET of Cyt-c (552) adsorbed onto electrodes coated with 
      mixed SAMs HS-(CH(2))( n )-CH(3)/HS-(CH(2))( n + 1)-OH 50/50, n = 5, 10 or 15, 
      respectively.
FAU - Bernad, Sophie
AU  - Bernad S
AD  - LADIR, CNRS/UPMC (UMR 7075), 2 rue Henri Dunant, 94320, Thiais, France.
FAU - Leygue, Nadine
AU  - Leygue N
FAU - Korri-Youssoufi, Hafsa
AU  - Korri-Youssoufi H
FAU - Lecomte, Sophie
AU  - Lecomte S
LA  - eng
PT  - Journal Article
DEP - 20070605
PL  - Germany
TA  - Eur Biophys J
JT  - European biophysics journal : EBJ
JID - 8409413
RN  - 0 (Cytochrome c Group)
RN  - 3M4G523W1G (Silver)
RN  - 9048-78-6 (cytochrome C-552)
SB  - IM
MH  - Biomimetic Materials
MH  - Cytochrome c Group/chemistry/*metabolism
MH  - Electrochemistry
MH  - Electrodes
MH  - Electron Transport/*physiology
MH  - Kinetics
MH  - Silver
MH  - Spectrum Analysis, Raman
MH  - Thermus thermophilus/chemistry
EDAT- 2007/06/06 09:00
MHDA- 2008/03/26 09:00
CRDT- 2007/06/06 09:00
PHST- 2007/02/14 00:00 [received]
PHST- 2007/04/24 00:00 [accepted]
PHST- 2007/04/23 00:00 [revised]
PHST- 2007/06/06 09:00 [pubmed]
PHST- 2008/03/26 09:00 [medline]
PHST- 2007/06/06 09:00 [entrez]
AID - 10.1007/s00249-007-0173-z [doi]
PST - ppublish
SO  - Eur Biophys J. 2007 Nov;36(8):1039-48. doi: 10.1007/s00249-007-0173-z. Epub 2007 
      Jun 5.