Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism

Jun Wang, Gizem Keceli, Rui Cao, Jiangtao Su, Zhiyuan Mi

Research output: Contribution to journalReview articlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)17-25
Number of pages9
JournalRedox Report
Issue number1
StatePublished - Jan 2 2017


  • EPR
  • Molybdenum-containing enzymes
  • Nitric oxide
  • Nitrite reductase
  • UV–vis
  • X-ray

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Clinical Biochemistry
  • Cell Biology
  • Biochemistry, medical


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