Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates.

@article{Costas2004DioxygenAA,
  title={Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates.},
  author={M. Costas and M. Mehn and M. Jensen and L. Que},
  journal={Chemical reviews},
  year={2004},
  volume={104 2},
  pages={
          939-86
        }
}

Topics from this paper

Catalytic diversity of cupin domain-containing enzymes
Catalytic bleaching of cotton: molecular and macroscopic aspects
Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis.
Nitrosyl hydride (HNO) replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase
Dioxygenases in Burkholderia ambifaria and Yersinia pestis that hydroxylate the outer Kdo unit of lipopolysaccharide
...
1
2
3
4
5
...