Journal of Biological Inorganic Chemistry
The active sites of metalloenzymes that catalyze O2-dependent reactions generally contain iron or copper ions. However, several enzymes are capable of activating O2 at manganese or nickel centers instead, and a handful of dioxygenases exhibit activity when substituted with cobalt. This minireview summarizes the catalytic properties of oxygenases and oxidases with mononuclear Mn, Co, or Ni active sites, including oxalate-degrading oxidases, catechol dioxygenases, and quercetin dioxygenase. In addition, recent developments in the O2 reactivity of synthetic Mn, Co, or Ni complexes are described, with an emphasis on the nature of reactive intermediates featuring superoxo-, peroxo-, or oxo-ligands. Collectively, the biochemical and synthetic studies discussed herein reveal the possibilities and limitations of O2 activation at these three “overlooked” metals.
Fiedler, Adam T. and Fischer, Anne A., "Oxygen Activation by Mononuclear Mn, Co, and Ni Centers in Biology and Synthetic Complexes" (2017). Chemistry Faculty Research and Publications. 535.
Accepted version. Journal of Biological Inorganic Chemistry, Vol. 22, No. 2-3 (April 2017): 407-424. DOI. © 2017 Springer International Publishing AG. Part of Springer Nature. Used with permission.
Shareable Link. Provided by the Springer Nature SharedIt content-sharing initiative.