Spectroelectrochemistry of cytochrome P450cam
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/139722
- author
- Bistolas, Nikitas ; Christenson, Andreas LU ; Ruzgas, Tautgirdas LU ; Jung, Christiane ; Scheller, Frieder and Wollenberger, Ulla
- organization
- publishing date
- 2004
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- 2d2987a0-6b16-46e8-9c00-9523cd6c710b (old id 139722)
- date added to LUP
- 2016-04-01 16:22:42
- date last changed
- 2022-01-28 19:17:44
@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}}, doi = {{10.1016/j.bbrc.2003.12.159}}, volume = {{314}}, year = {{2004}}, }