An Ultracentrifugal Approach to Quantitative Characterization of the Molecular Assembly of a Physiological Electron‐Transfer Complex. The Interaction of Electron‐Transferring Flavoprotein with Trimethylamine Dehydrogenase
The interaction between two physiological redox partners, trimethylamine dehydrogenase and electron‐transferring flavoprotein, has been characterized quantitatively by analytical ultracentrifugation at 4°C. Analysis of sedimentation‐equilibrium distributions obtained at 15000 rpm for mixtures in 10...
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| Veröffentlicht in: | European journal of biochemistry 1997-01, Vol.243 (1‐2), p.393-399 |
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| container_end_page | 399 |
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| container_issue | 1‐2 |
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| container_title | European journal of biochemistry |
| container_volume | 243 |
| creator | Wilson, Emma K. Scrutton, Nigel S. Cölfen, Helmut Harding, Stephen E. Jacobsen, Michael P. Winzor, Donald J. |
| description | The interaction between two physiological redox partners, trimethylamine dehydrogenase and electron‐transferring flavoprotein, has been characterized quantitatively by analytical ultracentrifugation at 4°C. Analysis of sedimentation‐equilibrium distributions obtained at 15000 rpm for mixtures in 10 mM potassium phosphate, pH 7.5, by means of the psi function [Wills, P. R., Jacobsen, M. P. & Winzor, D. J. (1996) Biopolymers 38, 119–1301 has yielded an intrinsic dissociation constant of 3–7 μM for the interaction of electron‐transferring flavoprotein with two equivalent and independent sites on the homodimeric enzyme. This investigation indicates the potential of sedimentation equilibrium for the quantitative characterization of interactions between dissimilar macromolecules. |
| doi_str_mv | 10.1111/j.1432-1033.1997.0393a.x |
| format | Article |
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The Interaction of Electron‐Transferring Flavoprotein with Trimethylamine Dehydrogenase</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The interaction between two physiological redox partners, trimethylamine dehydrogenase and electron‐transferring flavoprotein, has been characterized quantitatively by analytical ultracentrifugation at 4°C. Analysis of sedimentation‐equilibrium distributions obtained at 15000 rpm for mixtures in 10 mM potassium phosphate, pH 7.5, by means of the psi function [Wills, P. R., Jacobsen, M. P. & Winzor, D. J. (1996) Biopolymers 38, 119–1301 has yielded an intrinsic dissociation constant of 3–7 μM for the interaction of electron‐transferring flavoprotein with two equivalent and independent sites on the homodimeric enzyme. This investigation indicates the potential of sedimentation equilibrium for the quantitative characterization of interactions between dissimilar macromolecules.</description><subject>analytical ultracentrifugation</subject><subject>Bacteria - enzymology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Electron Transport</subject><subject>Electron-Transferring Flavoproteins</subject><subject>electron‐transfer flavoprotein</subject><subject>Flavoproteins - chemistry</subject><subject>Macromolecular Substances</subject><subject>Oxidoreductases, N-Demethylating - chemistry</subject><subject>Protein Binding</subject><subject>protein interaction</subject><subject>trimethylamine dehydrogenase</subject><subject>Ultracentrifugation</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcGO0zAURSMEGjoDn4DkFbsGu04TZ4MUSgsjDQJEZ205zkvjyrGL7cw0rOYT-EX4EhxazYoF3tjyve-8K90kQQSnJJ43-5RkdDEnmNKUlGWRYlpSkR6fJLNH4Wkyw5hk80W5zJ8nl97vMcZ5mRcXyUWJKS7ybJb8qgy61cEJCSY41Q47oVF1ODgrZIeCRV8HYYIKIqg7QKtORGcAp37ED2uQbVHoAH2yGuSghUOV99DXepwUgb50o1dW252SEbuOpuCs-f3wc-uE8S04tLL9QcMxRduIuTYRHfln8j_8Tpkd2mhxZ2PCAMqgexU6tHWqh9CNWvTKAHoP3dg4uwMjPLxInrVCe3h5vq-S2816u_o4v_n84XpV3cxlRpbVvJZZXjQlFG2dZYyJjBQZJY1slpgVGYimLSWRVIKogdUlwzXL2xovainixHJBr5LXJ25M9n0AH3ivvASthQE7eF4wRiljOBrZySid9d5Byw8xvnAjJ5hP7fI9n0rkU4l8apf_bZcf4-ir846h7qF5HDzXGfW3J_1eaRj_m8s363ff4rOifwCKM757</recordid><startdate>19970115</startdate><enddate>19970115</enddate><creator>Wilson, Emma K.</creator><creator>Scrutton, Nigel S.</creator><creator>Cölfen, Helmut</creator><creator>Harding, Stephen E.</creator><creator>Jacobsen, Michael P.</creator><creator>Winzor, Donald J.</creator><general>Blackwell Science Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19970115</creationdate><title>An Ultracentrifugal Approach to Quantitative Characterization of the Molecular Assembly of a Physiological Electron‐Transfer Complex. The Interaction of Electron‐Transferring Flavoprotein with Trimethylamine Dehydrogenase</title><author>Wilson, Emma K. ; Scrutton, Nigel S. ; Cölfen, Helmut ; Harding, Stephen E. ; Jacobsen, Michael P. ; Winzor, Donald J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415A-bc467d9e7fb4488a417431dcd50874eadf9c1c3ceabe8b980b86fb02bcafb4523</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>analytical ultracentrifugation</topic><topic>Bacteria - enzymology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Electron Transport</topic><topic>Electron-Transferring Flavoproteins</topic><topic>electron‐transfer flavoprotein</topic><topic>Flavoproteins - chemistry</topic><topic>Macromolecular Substances</topic><topic>Oxidoreductases, N-Demethylating - chemistry</topic><topic>Protein Binding</topic><topic>protein interaction</topic><topic>trimethylamine dehydrogenase</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilson, Emma K.</creatorcontrib><creatorcontrib>Scrutton, Nigel S.</creatorcontrib><creatorcontrib>Cölfen, Helmut</creatorcontrib><creatorcontrib>Harding, Stephen E.</creatorcontrib><creatorcontrib>Jacobsen, Michael P.</creatorcontrib><creatorcontrib>Winzor, Donald J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilson, Emma K.</au><au>Scrutton, Nigel S.</au><au>Cölfen, Helmut</au><au>Harding, Stephen E.</au><au>Jacobsen, Michael P.</au><au>Winzor, Donald J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An Ultracentrifugal Approach to Quantitative Characterization of the Molecular Assembly of a Physiological Electron‐Transfer Complex. 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| ispartof | European journal of biochemistry, 1997-01, Vol.243 (1‐2), p.393-399 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | Wiley Online Library - AutoHoldings Journals; MEDLINE; Alma/SFX Local Collection |
| subjects | analytical ultracentrifugation Bacteria - enzymology Bacterial Proteins - chemistry Electron Transport Electron-Transferring Flavoproteins electron‐transfer flavoprotein Flavoproteins - chemistry Macromolecular Substances Oxidoreductases, N-Demethylating - chemistry Protein Binding protein interaction trimethylamine dehydrogenase Ultracentrifugation |
| title | An Ultracentrifugal Approach to Quantitative Characterization of the Molecular Assembly of a Physiological Electron‐Transfer Complex. The Interaction of Electron‐Transferring Flavoprotein with Trimethylamine Dehydrogenase |
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