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Spectroelectrochemistry of cytochrome P450cam

Bistolas, Nikitas; Christenson, Andreas LU ; Ruzgas, Tautgirdas LU ; Jung, Christiane; Scheller, Frieder and Wollenberger, Ulla (2004) In Biochemical and Biophysical Research Communications 314(3). p.810-816
Abstract
The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4′-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV–visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4′-dithiodipyridin and dithionite modified electrodes. A formal potential (E0′) of −373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during... (More)
The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4′-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV–visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4′-dithiodipyridin and dithionite modified electrodes. A formal potential (E0′) of −373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
314
issue
3
pages
810 - 816
publisher
Elsevier
external identifiers
  • wos:000188613100023
  • pmid:14741708
  • scopus:1642497608
ISSN
1090-2104
DOI
10.1016/j.bbrc.2003.12.159
language
English
LU publication?
yes
id
2d2987a0-6b16-46e8-9c00-9523cd6c710b (old id 139722)
date added to LUP
2007-06-26 12:59:35
date last changed
2017-01-01 07:03:39
@article{2d2987a0-6b16-46e8-9c00-9523cd6c710b,
  abstract     = {The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4′-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV–visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4′-dithiodipyridin and dithionite modified electrodes. A formal potential (E0′) of −373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis},
  author       = {Bistolas, Nikitas and Christenson, Andreas and Ruzgas, Tautgirdas and Jung, Christiane and Scheller, Frieder and Wollenberger, Ulla},
  issn         = {1090-2104},
  language     = {eng},
  number       = {3},
  pages        = {810--816},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Spectroelectrochemistry of cytochrome P450cam},
  url          = {http://dx.doi.org/10.1016/j.bbrc.2003.12.159},
  volume       = {314},
  year         = {2004},
}