2010
DOI: 10.1039/b925331a
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Cytochrome c covalently immobilized on mesoporous silicas as a peroxidase: Orientation effect

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Cited by 43 publications
(40 citation statements)
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“…If the active site or its opening are oriented towards the pore wall, the substrate accessibility will be limited; hence, a lower enzyme activity. This was also shown through surface modifications of a mesoporous material that in the model could be used to selectively control the orientation of a peroxidase [47]. The surface had been modified with three different linkers binding to different sites on the enzyme, which caused different orientations of the enzyme upon binding to the linker.…”
Section: Protein Modeling and Molecular Dynamics Simulationsmentioning
confidence: 97%
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“…If the active site or its opening are oriented towards the pore wall, the substrate accessibility will be limited; hence, a lower enzyme activity. This was also shown through surface modifications of a mesoporous material that in the model could be used to selectively control the orientation of a peroxidase [47]. The surface had been modified with three different linkers binding to different sites on the enzyme, which caused different orientations of the enzyme upon binding to the linker.…”
Section: Protein Modeling and Molecular Dynamics Simulationsmentioning
confidence: 97%
“…In relation to enzyme immobilization this allows protein modeling of the enzyme structure and calculation of surface potential or charge distribution on the surface at different pH (see Figure 9) [9,47,108,113]. This information can partly be used to predict how strongly enzymes can bind to the surface and how the strength depends on the environmental conditions upon immobilization [9].…”
Section: Protein Modeling and Molecular Dynamics Simulationsmentioning
confidence: 99%
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