Fluorescence Lifetime Analysis of Nitrite Reductase from Alcaligenes xylosoxidans at the Single-Molecule Level Reveals the Enzyme Mechanism

被引：20

作者：

Tabares, Leandro C. ^{[2
]}

Kostrz, Dorota ^{[1
]}

Elmalk, Abdalmohsen ^{[2
]}

Andreoni, Alessio ^{[2
]}

Dennison, Christopher ^{[1
]}

Aartsma, Thijs J. ^{[2
]}

Canters, Gerard W. ^{[2
]}

机构：

[1] Newcastle Univ, Inst Cell & Mol Biosci, Sch Med, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England

[2] Leiden Univ, Leiden Inst Phys, Huygens Lab, NL-2333 CA Leiden, Netherlands

来源：

CHEMISTRY-A EUROPEAN JOURNAL | 2011年 / 17卷 / 43期

关键词：

copper; electron transfer; oxidoreductases; random sequential mechanism; single-molecule studies; TYPE-2; COPPER; ACTIVE-SITE; ORDERED MECHANISM; ELECTRON-TRANSFER; PH-DEPENDENCE; RESIDUES; DENITRIFICATION; KINETICS; BINDING; STATE;

D O I：

10.1002/chem.201102063

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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). © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：12015 / 12019

页数：5

共 7 条

[1] The enzyme mechanism of nitrite reductase studied at single-molecule level
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