Gardner Paul R
Department of Chemistry, University of Dayton, Dayton, Ohio, USA.
Methods Enzymol. 2008;436:217-37. doi: 10.1016/S0076-6879(08)36012-1.
A variety of hemoglobins, including several microbial flavohemoglobins, enzymatically dioxygenate the free radical nitric oxide (*NO) to form nitrate. Many of these *NO dioxygenases have been shown to control *NO toxicity and signaling. Furthermore, *NO dioxygenation appears to be an ancient and intrinsic function for members of the hemoglobin superfamily found in Archaea, eukaryotes, and bacteria. Yet for many hemoglobins, a function remains to be elucidated. Methods for the assay and characterization of the *NO dioxygenase (EC 1.14.12.17) activity and function of flavohemoglobins are described. The methods may also be applied to the discovery and design of inhibitors for use as antibiotics or as modulators of *NO signaling.
多种血红蛋白，包括几种微生物黄素血红蛋白，可通过酶促作用将自由基一氧化氮（NO）双加氧生成硝酸盐。已证明许多这类NO双加氧酶可控制NO的毒性和信号传导。此外，NO双加氧作用似乎是古菌、真核生物和细菌中血红蛋白超家族成员的一种古老而内在的功能。然而，对于许多血红蛋白来说，其功能仍有待阐明。本文描述了黄素血红蛋白NO双加氧酶（EC 1.14.12.17）活性和功能的测定及表征方法。这些方法也可应用于发现和设计用作抗生素或NO信号调节剂的抑制剂。
