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- Publisher Website: 10.1016/S0076-6879(09)63042-1
- Scopus: eid_2-s2.0-71549142859
- PMID: 19892202
- WOS: WOS:000272201000042
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Article: Chapter 42 Techniques to Isolate O2-Sensitive Proteins. [4Fe-4S]-FNR as an Example
Title | Chapter 42 Techniques to Isolate O2-Sensitive Proteins. [4Fe-4S]-FNR as an Example |
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Other Titles | Techniques to isolate O2-sensitive proteins: [4Fe-4S]-FNR as an example |
Authors | |
Issue Date | 2009 |
Publisher | Academic Press. The Journal's web site is located at http://www.sciencedirect.com/science/bookseries/00766879 |
Citation | Methods In Enzymology, 2009, v. 463 C, p. 787-805 How to Cite? |
Abstract | Many key enzymes in biological redox reactions require metal centers or cofactors for optimum activity and function. While the metal centers provide unique properties for protein structure and function, some also render protein activity sensitive to environmental O2 and cause experimental challenges to isolation and biochemical analysis. Iron-sulfur (Fe-S) clusters represent an important class of such metal centers and Fe-S proteins are widely distributed in nature. Here, we utilize FNR, a regulatory Fe-S protein from Escherichia coli, as an example to describe the techniques essential to purifying O2-labile proteins and summarize various approaches for their biochemical analysis. These methods can be readily adapted to purify other O2-labile proteins and advance our understanding of this interesting class of proteins. © 2009 Elsevier Inc. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/179170 |
ISSN | 2021 Impact Factor: 1.682 2023 SCImago Journal Rankings: 0.133 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Yan, A | en_US |
dc.contributor.author | Kiley, PJ | en_US |
dc.date.accessioned | 2012-12-19T09:52:31Z | - |
dc.date.available | 2012-12-19T09:52:31Z | - |
dc.date.issued | 2009 | en_US |
dc.identifier.citation | Methods In Enzymology, 2009, v. 463 C, p. 787-805 | en_US |
dc.identifier.issn | 0076-6879 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/179170 | - |
dc.description.abstract | Many key enzymes in biological redox reactions require metal centers or cofactors for optimum activity and function. While the metal centers provide unique properties for protein structure and function, some also render protein activity sensitive to environmental O2 and cause experimental challenges to isolation and biochemical analysis. Iron-sulfur (Fe-S) clusters represent an important class of such metal centers and Fe-S proteins are widely distributed in nature. Here, we utilize FNR, a regulatory Fe-S protein from Escherichia coli, as an example to describe the techniques essential to purifying O2-labile proteins and summarize various approaches for their biochemical analysis. These methods can be readily adapted to purify other O2-labile proteins and advance our understanding of this interesting class of proteins. © 2009 Elsevier Inc. All rights reserved. | en_US |
dc.language | eng | en_US |
dc.publisher | Academic Press. The Journal's web site is located at http://www.sciencedirect.com/science/bookseries/00766879 | en_US |
dc.relation.ispartof | Methods in Enzymology | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Bacteriological Techniques - Methods | en_US |
dc.subject.mesh | Cell Fractionation - Methods | en_US |
dc.subject.mesh | Drug Resistance - Physiology | en_US |
dc.subject.mesh | Escherichia Coli Proteins - Analysis - Isolation & Purification | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Iron-Sulfur Proteins - Analysis - Isolation & Purification | en_US |
dc.subject.mesh | Models, Biological | en_US |
dc.subject.mesh | Oxygen - Pharmacology | en_US |
dc.subject.mesh | Proteins - Chemistry - Drug Effects - Isolation & Purification | en_US |
dc.title | Chapter 42 Techniques to Isolate O2-Sensitive Proteins. [4Fe-4S]-FNR as an Example | en_US |
dc.title.alternative | Techniques to isolate O2-sensitive proteins: [4Fe-4S]-FNR as an example | - |
dc.type | Article | en_US |
dc.identifier.email | Yan, A: ayan8@hku.hk | en_US |
dc.identifier.authority | Yan, A=rp00823 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1016/S0076-6879(09)63042-1 | en_US |
dc.identifier.pmid | 19892202 | - |
dc.identifier.scopus | eid_2-s2.0-71549142859 | en_US |
dc.identifier.hkuros | 220835 | - |
dc.identifier.hkuros | 159702 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-71549142859&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 463 | en_US |
dc.identifier.issue | C | en_US |
dc.identifier.spage | 787 | en_US |
dc.identifier.epage | 805 | en_US |
dc.identifier.isi | WOS:000272201000042 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Yan, A=8621667000 | en_US |
dc.identifier.scopusauthorid | Kiley, PJ=7003423944 | en_US |
dc.identifier.issnl | 0076-6879 | - |