High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor
Cytochrome c is one of the most studied proteins probably due to its electron‐transfer properties in aerobic and anaerobic respiration. Particularly, cytochrome c from bovine heart is a small protein, Mr 12,230 Da, globular (hydrodynamic diameter of 3.4 nm), soluble in different buffer solutions, an...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2008-01, Vol.70 (1), p.83-92 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Mirkin, Nurit Jaconcic, Jean Stojanoff, Vivian Moreno, Abel |
| description | Cytochrome c is one of the most studied proteins probably due to its electron‐transfer properties in aerobic and anaerobic respiration. Particularly, cytochrome c from bovine heart is a small protein, Mr 12,230 Da, globular (hydrodynamic diameter of 3.4 nm), soluble in different buffer solutions, and commercially available. Despite being a quite well‐studied protein and relatively easy to manipulate from the biochemical and electrochemical viewpoint, its 3D structure has never been published. In this work, the purification, crystallization and 3D structure of one of the cytochrome c isoforms is presented to 1.5 Å resolution. It is also shown how the presence of isoforms made both the purification and crystallization steps difficult. Finally, a new approach for protein electrocrystallization and design of biosensors is presented. Proteins 2008. © 2007 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/prot.21452 |
| format | Article |
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Particularly, cytochrome c from bovine heart is a small protein, Mr 12,230 Da, globular (hydrodynamic diameter of 3.4 nm), soluble in different buffer solutions, and commercially available. Despite being a quite well‐studied protein and relatively easy to manipulate from the biochemical and electrochemical viewpoint, its 3D structure has never been published. In this work, the purification, crystallization and 3D structure of one of the cytochrome c isoforms is presented to 1.5 Å resolution. It is also shown how the presence of isoforms made both the purification and crystallization steps difficult. Finally, a new approach for protein electrocrystallization and design of biosensors is presented. 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Proteins 2008. © 2007 Wiley‐Liss, Inc.</description><subject>Animals</subject><subject>atomic force microscopy</subject><subject>Biosensing Techniques</subject><subject>Cattle</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Crystallography, X-Ray</subject><subject>cytochrome c from bovine heart mitochondria</subject><subject>Cytochromes c - chemistry</subject><subject>Electrochemistry</subject><subject>electrocrystallization</subject><subject>Electron Transport</subject><subject>gel acupuncture method</subject><subject>Microscopy, Atomic Force</subject><subject>Myocardium - enzymology</subject><subject>Protein Conformation</subject><subject>Scattering, Radiation</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>X-ray diffraction</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFu1DAURS0EokNhwwcgr1ggpfjZcZwsaQUtVdUiVCg7y3FeJoZMHGwHyGfwx510pmXH6i3euWdxLyEvgR0BY_ztGHw64pBL_oisgFUqYyDyx2TFylJlQpbygDyL8TtjrKhE8ZQcgCpEXpWwIn_P3LqjAaPvp-T8QL9lwczUhjkm0_d-HczYOUtjCpNNU0DqW1r7X25A2qEJido5edsFv0FqqRka6lKkZhx7Z82dMXmaOqQNRrcelrgZKPZoU1iewQyxxUBr5yMO0Yfn5Elr-ogv9veQfPnw_vrkLLu4Ov148u4is7kAnqHlkskaOCvquqhNhYUElEoqaHNuioZb0wAYBiUv8qpVOZeYQ10qnnMohTgkr3febX0_J4xJb1y02PdmQD9FrdjSUiW34JsdaIOPMWCrx-A2JswamF4G0MsA-m6ALfxqb53qDTb_0H3jWwB2wG_X4_wflf70-er6XprtMi4m_POQMeGHLpRQUt9cnmq4-Xp8fK6YvhS3nj2ieg</recordid><startdate>200801</startdate><enddate>200801</enddate><creator>Mirkin, Nurit</creator><creator>Jaconcic, Jean</creator><creator>Stojanoff, Vivian</creator><creator>Moreno, Abel</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><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>200801</creationdate><title>High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor</title><author>Mirkin, Nurit ; Jaconcic, Jean ; Stojanoff, Vivian ; Moreno, Abel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4312-ec2505b1206bb6ba9e651e57571f42a6d2cad11a0182649f7425e41b872421833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>atomic force microscopy</topic><topic>Biosensing Techniques</topic><topic>Cattle</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Crystallography, X-Ray</topic><topic>cytochrome c from bovine heart mitochondria</topic><topic>Cytochromes c - chemistry</topic><topic>Electrochemistry</topic><topic>electrocrystallization</topic><topic>Electron Transport</topic><topic>gel acupuncture method</topic><topic>Microscopy, Atomic Force</topic><topic>Myocardium - enzymology</topic><topic>Protein Conformation</topic><topic>Scattering, Radiation</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mirkin, Nurit</creatorcontrib><creatorcontrib>Jaconcic, Jean</creatorcontrib><creatorcontrib>Stojanoff, Vivian</creatorcontrib><creatorcontrib>Moreno, Abel</creatorcontrib><collection>Istex</collection><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>Proteins, structure, function, and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mirkin, Nurit</au><au>Jaconcic, Jean</au><au>Stojanoff, Vivian</au><au>Moreno, Abel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>2008-01</date><risdate>2008</risdate><volume>70</volume><issue>1</issue><spage>83</spage><epage>92</epage><pages>83-92</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>Cytochrome c is one of the most studied proteins probably due to its electron‐transfer properties in aerobic and anaerobic respiration. 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| identifier | ISSN: 0887-3585 |
| ispartof | Proteins, structure, function, and bioinformatics, 2008-01, Vol.70 (1), p.83-92 |
| issn | 0887-3585 1097-0134 |
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| subjects | Animals atomic force microscopy Biosensing Techniques Cattle Chromatography, High Pressure Liquid Crystallography, X-Ray cytochrome c from bovine heart mitochondria Cytochromes c - chemistry Electrochemistry electrocrystallization Electron Transport gel acupuncture method Microscopy, Atomic Force Myocardium - enzymology Protein Conformation Scattering, Radiation Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization X-ray diffraction |
| title | High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor |
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