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Spectroscopic and computational insight into the activation of O2 by the mononuclear Cu center in polysaccharide monooxygenases.
Spectroscopic and computational insight into the activation of O2 by the mononuclear Cu center in polysaccharide monooxygenases.
- Source :
- Proceedings of the National Academy of Sciences of the United States of America; 6/17/2014, Vol. 111 Issue 24, p8797-8802, 6p
- Publication Year :
- 2014
-
Abstract
- Strategies for O<subscript>2</subscript> activation by copper enzymes were recently expanded to include mononuclear Cu sites, with the discovery of the copper-dependent polysaccharide monooxygenases, also classified as auxiliary-activity enzymes 9-11 (AA9-11). These enzymes are finding considerable use in industrial biofuel production. Crystal structures of polysaccharide monooxygenases have emerged, but experimental studies are yet to determine the solution structure of the Cu site and how this relates to reactivity. From X-ray absorption near edge structure and extended X-ray absorption fine structure spectroscopies, we observed a change from four-coordinate Cu(ll) to three-coordinate Cu(l) of the active site in solution, where three protein-derived nitrogen ligands coordinate the Cu in both redox states, and a labile hydroxide ligand is lost upon reduction. The spectroscopic data allowed for density functional theory calculations of an enzyme active site model, where the optimized Cu(l) and (II) structures were consistent with the experimental data. The O<subscript>2</subscript> reactivity of the Cu(l) site was probed by EPR and stopped-flow absorption spectroscopies, and a rapid one-electron reduction of O<subscript>2</subscript> and regeneration of the resting Cu(ll) enzyme were observed. This reactivity was evaluated computationally, and by calibration to Cu-superoxide model complexes, formation of an end-on Cu-AA9-superoxide species was found to be thermodynamically favored. We discuss how this thermodynamically difficult one-electron reduction of O<subscript>2</subscript> is enabled by the unique protein structure where two nitrogen ligands from His1 dictate formation of a T-shaped Cu(l) site, which provides an open coordination position for strong O<subscript>2</subscript> binding with very little reorganization energy. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00278424
- Volume :
- 111
- Issue :
- 24
- Database :
- Complementary Index
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 96808327
- Full Text :
- https://doi.org/10.1073/pnas.1408115111