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Health, Safety & Environment

Nitrite reductase

Molybdenum-containing Nitrite reductases: Spectroscopic characterization and redox mechanism

Objectives: This review summarizes the spectroscopic results, which will provide useful suggestions for future research. In addition, the fields that urgently need more information are also advised.

Background: Nitrite-NO-cGMP has been considered as an important signaling pathway of NO in human cells. To date, all the four known human molybdenum-containing enzymes, xanthine oxidase, aldehyde oxidase, sulfite oxidase, and mitochondrial amidoxime-reducing component, have been shown to function as nitrite reductases under hypoxia by biochemical, cellular, or animal studies. Various spectroscopic techniques have been applied to investigate the structure and catalytic mechanism of these enzymes for more than 20 years.

Methods: We summarize the published data on the applications of UV-vis and EPR spectroscopies, and X-ray crystallography in studying nitrite reductase activity of the four human molybdenum-containing enzymes.

Results: UV-vis has provided useful information on the redox active centers of these enzymes. The utilization of EPR spectroscopy has been critical in determining the coordination and redox status of the Mo center during catalysis. Despite the lack of substrate-bound crystal structures of these nitrite reductases, valuable structural information has been obtained by X-ray crystallography.

Conclusions: To fully understand the catalytic mechanisms of these physiologically/pathologically important nitrite reductases, structural studies on substrate-redox center interaction are needed.

Wang, J., Keceli, G., Cao, R., Su, J., and Mi, Z.,Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism, Redox report : communications in free radical research, 2017, 22, 17-25.

Nitric oxide (NO) is a signalling molecule involved in several physiological processes, in both prokaryotes and eukaryotes, and nitrite is being recognised as an NO source particularly relevant to cell signalling and survival under challenging conditions. The "non-respiratory" nitrite reduction to NO is carried out by "non-dedicated" nitrite reductases, making use of metalloproteins present in cells to carry out other functions, such as several molybdoenzymes (a new class of nitric oxide-forming nitrite reductases). This minireview will highlight the physiological relevance of molybdenum-dependent nitrite-derived NO formation in mammalian, plant and bacterial signalling (and other) pathways. The mammalian xanthine oxidase/xanthine dehydrogenase, aldehyde oxidase, mitochondrial amidoxime-reducing component, plant nitrate reductase and bacterial aldehyde oxidoreductase and nitrate reductases will be considered. The nitrite reductase activity of each molybdoenzyme will be described and the review will be oriented to discuss the feasibility of the reactions from a (bio)chemical point of view. In addition, the molecular mechanism proposed for the molybdenum-dependent nitrite reduction will be discussed in detail.

Maia LB(1), Moura JJ. Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases. J Biol Inorg Chem. 2015 Mar;20(2):403-33. doi: 10.1007/s00775-014-1234-2. Epub 2015 Jan 15.

Users of the Database should be aware that inclusion of an abstract in the Database does not imply any IMOA endorsement of the accuracy or reliability of the reported data or the quality of a publication.