The Water Effect on the Kinetics of the Bovine Liver Catalase
Authors: Augusto Vicente Seixas, Flavio; Ribeiro da Silva, Milene; Tyago Murakami, Mario; Tosqui, Priscilla; Francisco Colombo, Marcio
Source: Protein and Peptide Letters, Volume 18, Number 9, September 2011 , pp. 879-885(7)
Publisher: Bentham Science Publishers
Abstract:Catalase is an enzyme that occurs in almost all aerobic organisms. Its main metabolic function is to prevent oxidative damage to tissues induced by hydrogen peroxide which is a strong oxidizing agent. Catalase is very effective in performing this task, since it has the highest turnover rate among all the enzymes. The properties of catalase have been investigated extensively for many years; however, the role of the solvent molecules in the catalytic reaction of this enzyme has not yet been investigated. Therefore, the objective of this work was to investigate the contribution of the solvent molecules on the catalytic reaction of bovine liver catalase with its substrate H2O2 by the osmotic stress method. As a probe for protein structural changes in solution, the differential number of water molecules released during the transition from free to bound form of the enzyme was measured. These assays were correlated with protein structural data provided by the SAXS technique and crystallographic structures of free and CN?? bonded enzymes. The results showed that the difference in surface accessible area of the crystal structures does not reflect the variation that is observed in solution. Moreover, catalase is not influenced by the solvent during the catalytic reaction, which represents a lower energy barrier to be crossed in the overall energetics of the reaction, a fact that contributes to the high turnover rate of catalase.
Keywords: Catalase; Gibbs-Duhem expression; Helico bacter pilory catalase; MARCCD detector; Mickaelis-Menten cons; Oligomerization; Protein Data Bank; SAXS technique; Wyman linkage equation; bovine liver catalase; catalytic reaction; enzyme kinetics; osmotic stress; osmotic stress method; oxoferryl species; protein allostery; quaternary structure; superimposition; thermodynamic parameters; water effect
Document Type: Research Article
Publication date: September 1, 2011
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.