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Fluorescence Lifetime Analysis of Nitrite Reductase from Alcaligenes xylosoxidans at the Single‐Molecule Level Reveals the Enzyme Mechanism
Author(s) -
Tabares Leandro C.,
Kostrz Dorota,
Elmalk Abdalmohsen,
Andreoni Alessio,
Dennison Christopher,
Aartsma Thijs J.,
Canters Gerard W.
Publication year - 2011
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201102063
Subject(s) - nitrite reductase , enzyme , nitrite , fluorescence , chemistry , molecule , reductase , fluorescence spectroscopy , enzyme kinetics , combinatorial chemistry , stereochemistry , biochemistry , biophysics , biology , active site , nitrate reductase , physics , organic chemistry , optics , nitrate
Lighting the route : Immobilized, fluorescently labeled bacterial nitrite reductase (NiR) has been studied during steady‐state turnover by using single‐molecule fluorescence lifetime imaging spectroscopy. With this method, two populations of single NiR molecules exhibiting different turnover rates can be distinguished. The two populations are tentatively connected by two enzymatic routes: the reduction‐first or the binding‐first pathway (see picture).