Abstract
It is demonstrated that engineered arginase with a single protruded site of cysteine deliberately placed away from its active centre by site-directed mutagenesis can facilitate its attachment on a gold-nanoparticle surface with atomic precision, resulting in no apparent loss in enzymatic activity.
MeSH terms
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Adsorption
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Antineoplastic Agents / chemical synthesis*
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Arginase / chemistry*
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Arginase / genetics
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Arginase / metabolism
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Arginine / metabolism*
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Bacillus / chemistry
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Bacillus / enzymology
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Bacillus / genetics
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Cysteine / chemistry
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Electrochemistry
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Electrophoresis, Polyacrylamide Gel
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Enzymes, Immobilized / chemistry*
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Enzymes, Immobilized / genetics
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Enzymes, Immobilized / metabolism
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Gold / chemistry
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Kinetics
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Microscopy, Atomic Force
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Mutagenesis, Site-Directed
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Nanotubes, Carbon / chemistry
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Protein Engineering
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Surface Properties
Substances
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Antineoplastic Agents
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Bacterial Proteins
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Enzymes, Immobilized
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Nanotubes, Carbon
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Recombinant Proteins
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Gold
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Arginine
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Arginase
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Cysteine