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Bioelectrocatalytic Detection of Histamine Using Quinohemoprotein Amine Dehydrogenase and the Native Electron Acceptor Cytochrome c‐550
Author(s) -
Yamamoto Keiko,
Takagi Kazuyoshi,
Kano Kenji,
Ikeda Tokuji
Publication year - 2001
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/1521-4109(200104)13:5<375::aid-elan375>3.0.co;2-r
Subject(s) - electron transfer , chemistry , cytochrome c , histamine , biosensor , electron acceptor , acceptor , substrate (aquarium) , electron transport chain , redox , cytochrome , cytochrome b5 , amine gas treating , photochemistry , enzyme , inorganic chemistry , biochemistry , organic chemistry , biology , mitochondrion , ecology , physics , condensed matter physics , endocrinology
Abstract Bioelectrocatalytic sensor of histamine has been constructed using quinohemoprotein amine dehydrogenase (QH‐AmDH) as an enzyme and its native electron acceptor cytochrome c‐550 (Cyt c‐550) as a mediator. Highly reversible electron transfer of Cyt c‐550 is achieved at bis(4‐pyridyl)disulfide‐modified Au electrodes. The electron transfer from substrate‐reduced QH‐AmDH to oxidized Cyt c‐550 is in the diffusion‐controlled region, in spite of relatively small redox potential difference. QH‐AmDH and Cyt c‐550 can be co‐entrapped on the electrode surface with a suitable dialysis membrane. As a result, Cyt c‐550 is found to be an excellent mediator compared with other artificial ones. The sensor allows the histamine detection down to 500 nM ( S / N =3) and the linearity is retained up to 1.5 mM with a relative standard deviation of 4.8 % at 10 µM histamine ( n =6). The performance of the histamine biosensor is discussed in view of clinical chemistry.