Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-5-7
pubmed:abstractText
In this paper we explore the use of fluorescently labeled cytochrome c peroxidase (CcP) from baker's yeast for monitoring nitric oxide (NO) down to the sub-micromolar level, by means of a FRET (Förster Resonance Energy Transfer) mechanism. The binding affinity constant (K(d)) for the NO binding to CcP was determined to be 10+/-1.5 microM. The rate of NO dissociation from the CcP (k(off)) and the second order rate constant for the NO association (k(on)) were found to be 0.22+/-0.08 min(-1) and 0.024+/-0.002 microM(-1) min(-1) respectively. The immobilization of fluorescently labeled CcP into a polymeric matrix for use in a solid state NO sensing device was also explored. The results provide proof-of-principle that labeled CcP can be successfully implemented in a fast, simple, quantitative and sensitive NO sensing device.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1873-3344
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
619-24
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
A FRET-based biosensor for NO detection.
pubmed:affiliation
Dipartimento di Chimica, Università di Salerno, via Ponte Don Melillo, Fisciano (Sa), I84084 Italy.
pubmed:publicationType
Journal Article