Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Hayley A. Dash"'
Autor:
Adam Thetford, Natalie Bligh, Wojciech Nogala, Catherine M. Halliwell, Toby A. Jenkins, Hayley A. Dash, Frank Marken, Marcin Opallo, Elizabeth V. Milsom
Publikováno v:
Journal of Electroanalytical Chemistry. 610:28-36
Thin mesoporous nanocomposite films of SnO2–poly(diallyldimethylammonium chloride) are formed in a layer-by-layer deposition process from SnO2 nanoparticles (nominal 15 nm diameter) and poly(diallyldimethylammonium chloride) binder. Atomic force im
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f58f8c241f7e54d7c6c667364684bec0
https://doi.org/10.1016/j.jelechem.2007.06.021
https://doi.org/10.1016/j.jelechem.2007.06.021
Publikováno v:
Bioelectrochemistry (Amsterdam, Netherlands). 70(2)
Methemoglobin (bovine) is immobilized from aqueous phosphate buffer (pH 5.5) solution into thin porous TiO2 (anatase) films at ITO electrode surfaces. Films of TiO2 are produced in a deposition process employing 40 nm diameter TiO2 nanoparticles susp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c31812159e7dfb7e24c2e45e44bf5542
https://pubmed.ncbi.nlm.nih.gov/17056301
https://pubmed.ncbi.nlm.nih.gov/17056301
Autor:
A. Toby A. Jenkins, Richard H. ffrench-Constant, Catherine M. Halliwell, Sam Boundy, Hayley-Ann Dash
Publikováno v:
Bioelectrochemistry (Amsterdam, Netherlands). 68(1)
This paper describes the utilisation of methoxy-resorufin ether as an electrochemical probe for studying cytochrome P450 CYP6G1. Methoxy-resorufin ether is well established as a versatile substrate for cytochrome P450, as its demethylated product, re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b48e82dc270c50dc028455a51cefe29
https://pubmed.ncbi.nlm.nih.gov/15936991
https://pubmed.ncbi.nlm.nih.gov/15936991
Publikováno v:
Bioelectrochemistry. 72:1-2
Facile demetallation occurs upon contact of the methemoglobin with a mesoporous TiO2 host in phosphate buffer media at pH 5.5 but not in acetate buffer media. As a result, voltammetric signals previously attributed to hemoglobin-based redox processes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2813fc050cffa2d72ffa175b0028741f
https://doi.org/10.1016/j.bioelechem.2007.07.006
https://doi.org/10.1016/j.bioelechem.2007.07.006