Linked Life Data

12622383

Source:http://linkedlifedata.com/resource/pubmed/id/12622383

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-3-7
pubmed:abstractText
A series of glucose oxidase (GOx) hybrids (GOx-phe-nothiazine-labeled poly(ethylene oxide) (PT-PEO)) capable of direct electrical communication with electrodes is synthesized by covalently modifying PT-PEO to lysine residues on the enzyme surface. The length of the PEO chain and the number of PT groups are systematically altered. After the PT-PEO modification, all the hybrids maintain more than 50% of enzyme activity relative to that of native GOx, although loss of the activity becomes greater with increasing PEO chain length. The catalytic current, i(cat), is observed at a potential more positive than 0.55 V after the addition of glucose, due to the intramolecular electron transfer (El) from reduced forms of flavin adenine dinucletide (FADH2/FADH) to PT+ that are electrogenerated at the electrode. The i(cat) value increases with the number of PT groups, indicating that most of the modified PT groups act as mediators. The magnitude of the i(cat) increase depends on the PEO chain length and reveals a maximum for PT-PEO with the molecular weight of 3,000. In contrast, the i(cat) is almost constant for GOx-2-(10-phenothiazyl)propionic acid (PT-PA) hybrids with more than two PT groups synthesized by covalently modifying PT-PA to surface lysines, indicating that only a few key PT groups function as mediators. The maximum rate constant (130 s(-1)) for the ET from FADH2/FADH to PT+ is obtained for the GOx hybrid modified with five PT-PEO groups with the molecular weight of 3,000.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-2700
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
910-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Electrical communication between glucose oxidase and electrodes mediated by phenothiazine-labeled poly(ethylene oxide) bonded to lysine residues on the enzyme surface.
pubmed:affiliation
Department of Chemistry and Biotechnology, Yokohama National University, Yokohama 240-8501, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't