Clarke Thomas A, Mills Paul C, Poock Susie R, Butt Julea N, Cheesman Myles R, Cole Jeffrey A, Hinton Jay C D, Hemmings Andrew M, Kemp Gemma, Söderberg Christopher A G, Spiro Stephen, Van Wonderen Jessica, Richardson David J
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.
Methods Enzymol. 2008;437:63-77. doi: 10.1016/S0076-6879(07)37004-3.
The periplasmic cytochrome c nitrite reductase (Nrf) system of Escherichia coli utilizes nitrite as a respiratory electron acceptor by reducing it to ammonium. Nitric oxide (NO) is a proposed intermediate in this six-electron reduction and NrfA can use exogenous NO as a substrate. This chapter describes the method used to assay Nrf-catalyzed NO reduction in whole cells of E. coli and the procedures for preparing highly purified NrfA suitable for use in kinetic, spectroscopic, voltammetric, and crystallization studies.
大肠杆菌的周质细胞色素c亚硝酸还原酶（Nrf）系统通过将亚硝酸盐还原为铵，利用亚硝酸盐作为呼吸电子受体。一氧化氮（NO）被认为是这种六电子还原过程中的中间体，并且NrfA可以将外源性NO用作底物。本章描述了用于测定大肠杆菌全细胞中Nrf催化的NO还原的方法，以及制备适用于动力学、光谱学、伏安法和结晶学研究的高纯度NrfA的步骤。
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