Literature summary extracted from

Sezer, M.; Santos, A.; Kielb, P.; Pinto, T.; Martins, L.O.; Todorovic, S.
Distinct structural and redox properties of the heme active site in bacterial dye decolorizing peroxidase-type peroxidases from two subfamilies: resonance Raman and electrochemical study (2013), Biochemistry, 52, 3074-3084.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.11.1.16	resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the five-coordinated quantum mechanically mixed-spin state being the most populated in the latter. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -260 mV	Pseudomonas putida
1.11.1.19	resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the six-coordinated low-spin state being the most populated. The poor catalytic activity of BsDyP is ascribed to the presence of a catalytically incompetent six-coordinated low-spin population. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -40 mV at pH 7.6, which is substantially more positive than those reported for the majority of other peroxidases	Bacillus subtilis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.11.1.16	Pseudomonas putida	-	-	-
1.11.1.16	Pseudomonas putida MET94	-	-	-
1.11.1.19	Bacillus subtilis	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)