| Redox cycling and kinetic analysis of single molecules of solution-phase nitrite reductase. | |
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MedLine Citation:
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PMID: 21969548 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Single-molecule measurements are a valuable tool for revealing details of enzyme mechanisms by enabling observation of unsynchronized behavior. However, this approach often requires immobilizing the enzyme on a substrate, a process which may alter enzyme behavior. We apply a microfluidic trapping device to allow, for the first time, prolonged solution-phase measurement of single enzymes in solution. Individual redox events are observed for single molecules of a blue nitrite reductase and are used to extract the microscopic kinetic parameters of the proposed catalytic cycle. Changes in parameters as a function of substrate concentration are consistent with a random sequential substrate binding mechanism. |
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Authors:
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Randall H Goldsmith; Leandro C Tabares; Dorota Kostrz; Christopher Dennison; Thijs J Aartsma; G W Canters; W E Moerner |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. Date: 2011-10-03 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 108 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-19 Completed Date: 2011-12-30 Revised Date: 2012-04-18 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 17269-74 Citation Subset: IM |
Affiliation:
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Department of Chemistry, Stanford University, Stanford, CA 94305, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Alcaligenes
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enzymology,
genetics Amino Acid Substitution Bacterial Proteins / chemistry, genetics, metabolism Copper / chemistry Fluorescence Resonance Energy Transfer Kinetics Microfluidic Analytical Techniques Models, Molecular Mutagenesis, Site-Directed Nitrite Reductases / chemistry*, genetics, metabolism* Oxidation-Reduction Protein Structure, Quaternary Recombinant Proteins / chemistry, genetics, metabolism Solutions |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Recombinant Proteins; 0/Solutions; 7440-50-8/Copper; EC 1.7.-/Nitrite Reductases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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