М.П. Коломыцева

1. Kolomytseva M, Ferraroni M, Chernykh A, Golovleva L, Scozzafava A. Structural basis for the substrate specificity and the absence of dehalogenation activity in 2-chloromuconate cycloisomerase from Rhodococcus opacus 1CP. Biochim Biophys Acta. 2014 Apr 21. pii: S1570-9639(14)00094-6. doi: 10.1016/j.bbapap.2014.04.008. PMID:24768773

2. Ferraroni M, Kolomytseva M, Golovleva LA, Scozzafava A. X-ray crystallographic and molecular docking studies on a unique chloromuconolactone dehalogenase from Rhodococcus opacus 1CP. J Struct Biol. 2013, V. 182(1), pp. 44-50. doi: 10.1016/j.jsb.2013.01.006

3. Ferraroni M, Kolomytseva M, Scozzafava A, Golovleva L, Briganti F. X-ray structures of 4-chlorocatechol 1,2-dioxygenase adducts with substituted catechols: new perspectives in the molecular basis of intradiol ring cleaving dioxygenases specificity. J Struct Biol. 2013, V. 181(3), pp. 274-82. doi: 10.1016/j.jsb.2012.11.007

4. Ferraroni M., Matera I., Chernykh A., Kolomytseva M., Golovleva L., Scozzafava A., Briganti F. Reaction Intermediates and Redox State Changes in a Blue Laccase from Steccherinum ochraceum observed by Crystallographic High/Low X-Ray Dose Experiments. J Inorg Biochem, 2012, V. 111, pp. 203-209. doi: 10.1016/j.jinorgbio.2012.01.011

5. Kolomytseva M., Ferraroni M., Chernykh A.M., Scozzafava A., Briganti F., Golovleva L. Experimental and theoretical affinity studies of substituted phenols to chlorocatechol 1,2-dioxygenases: a step toward the comprehension of inhibitor/substrate binding to intradiol dioxygenases J Mol Cat B: Enzym, 2010, V. 64 (1-2), pp. 53-59. http://dx.doi.org/10.1016/j.molcatb.2010.02.001

6. Matera I., Ferraroni M., Kolomytseva M., Golovleva L., Scozzafava A., Briganti F. Catechol 1,2-dioxygenase from the Gram-positive Rhodococcus opacus 1CP: Quantitative structure/activity relationship and the crystal structures of native enzyme and catechols adducts. J Struct Biol, 2010, V. 170 (3), pp. 548-564. PMID: 20040374