Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 500, Issue 1, Pages 37-44Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2010.04.021
Keywords
Ab initio molecular dynamics; Density functional theory; Hydroperoxidases; Catalases; Peroxidases; Enzyme catalysis
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Funding
- Spanish Ministry of Science and Innovation (MICINN) [FIS2008-03845]
- Generalitat de Catalunya [2009SGR-1309]
- Natural Sciences and Engineering Research Council (NSERC) of Canada [9600]
- Canada Research Chair
- ICREA Funding Source: Custom
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The enzymatic cycle of hydroperoxidases involves the resting Fe(III) state of the enzyme and the high-valent iron intermediates Compound I and Compound II. These states might be characterized by X-ray crystallography and the transition pathways between each state can be investigated using atomistic simulations. Here we review our recent work in the modeling of two key steps of the enzymatic reaction of hydroperoxidases: the formation of Cpd I in peroxidase and the reduction of Cpd I in catalase. It will be shown that small conformational motions of distal side residues (His in peroxidases and His/Asn in catalases), not, or only partially, revealed by the available X-ray structures, play an important role in the catalytic processes examined. (C) 2010 Elsevier Inc. All rights reserved.
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