Title : Direct electron transfer of heme- and molybdopterin cofactor-containing chicken liver sulfite oxidase on alkanethiol-modified gold electrodes.

Pub. Date : 2003 Sep 15

PMID : 14674462






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Direct electron transfer of heme- and molybdopterin cofactor-containing chicken liver sulfite oxidase on alkanethiol-modified gold electrodes. alkanethiol sulfite oxidase Gallus gallus
2 Direct heterogeneous electron transfer (ET) of sulfite oxidase (SOx), a heme- and molybdopterin cofactor-containing intermembrane enzyme, was studied on alkanethiol-modified Au electrodes both with SOx entrapped between the modified Au electrode and a permselective membrane and with SOx adsorbed at the electrode surface, in the absence of any membrane. alkanethiol sulfite oxidase Gallus gallus
3 Direct heterogeneous electron transfer (ET) of sulfite oxidase (SOx), a heme- and molybdopterin cofactor-containing intermembrane enzyme, was studied on alkanethiol-modified Au electrodes both with SOx entrapped between the modified Au electrode and a permselective membrane and with SOx adsorbed at the electrode surface, in the absence of any membrane. alkanethiol sulfite oxidase Gallus gallus
4 The efficiency of the bioelectrocatalytic 2e- oxidation of sulfite catalyzed by SOx in direct ET exchange with the electrode was shown to depend essentially on the nature of the alkanethiol layer. alkanethiol sulfite oxidase Gallus gallus
5 Adsorption and orientation of SOx on an 11-mercapto-1-undecanol (MuD-OH) self-assembled monolayer, i.e., terminally functionalized with OH groups, provided efficient catalytic oxidation of sulfite, contrary to nonfunctionalized alkanethiols, e.g., 1-decanethiol, or alkanethiol layers terminally functionalized with NH2 groups. alkanethiol sulfite oxidase Gallus gallus