Correction to: The model structure of the copper-dependent ammonia Monooxygenase (JBIC Journal of Biological Inorganic Chemistry, (2020), 25, 7, (995-1007), 10.1007/s00775-020-01820-0)

In the original article published, the authors missed to acknowledging an article published by Liew et al. (Mutagenesis of the hydrocarbon monooxygenase indicates a metal centre in subunit-C, and not subunit-B, is essential for copper- containing membrane monooxygenase activity, Microbiology 2014, 160, 1267–1277). “Thus far, however, the crystal structures have not fully established the location and composition of the pMMO active site [48], but all evidence points to either the CuB or the CuC site for this role. It is the opinion of the authors of the present study that the latter, with its labile water-bound position, should more logically constitute the enzyme active metal site. This conclusion is strongly supported by site-directed mutagenesis studies on the copper-dependent hydrocarbon monooxygenase (HMO) from Mycobacterium NBB4 which provided the first evidence that the C site was essential for activity, whereas mutations in the B site impaired, but did not eliminate, activity (E. F. Liew, D. Tong, N. V. Coleman, A. J. Holmes, Microbiology 2014, 160, 1267–1277)”.