Characterization of perdeuterated high‐potential iron‐sulfur protein with high‐resolution X‐ray crystallography
Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high‐resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we d...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2020-02, Vol.88 (2), p.251-259 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Hanazono, Yuya Takeda, Kazuki Miki, Kunio |
| description | Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high‐resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X‐ray structure of perdeuterated high‐potential iron‐sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high‐resolution neutron crystallography. |
| doi_str_mv | 10.1002/prot.25793 |
| format | Article |
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However, there is shortage of evidence that the high‐resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X‐ray structure of perdeuterated high‐potential iron‐sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. 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However, there is shortage of evidence that the high‐resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X‐ray structure of perdeuterated high‐potential iron‐sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high‐resolution neutron crystallography.</description><subject>Bacterial Proteins - chemistry</subject><subject>Chromatiaceae - metabolism</subject><subject>Circular Dichroism</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Deuterium - chemistry</subject><subject>high resolution</subject><subject>HiPIP</subject><subject>Hydrogen atoms</subject><subject>Hydrogen Bonding</subject><subject>Iron</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>iron‐sulfur cluster</subject><subject>Models, Molecular</subject><subject>neutron crystallography</subject><subject>Neutrons</subject><subject>perdeuteration</subject><subject>Photosynthetic Reaction Center Complex Proteins - chemistry</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Sulfur</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc9q3DAQh0VpSDZ_Ln2AYuilBJxIHluSj2Vp0kIgIewhNyHbcqygtVxJZnFOeYQ8Y54kcna3hx560mj4-Gb4DUJfCL4gGGeXg7PhIitYCZ_QguCSpZhA_hktMOcshYIXR-jY-yeMMS2BHqIjIEALUrAF2iw76WQdlNPPMmjbJ7ZNBuUaNcaeDKpJOv3Yvb28DjaoPmhpEu1sHxt-NO3oknm60n2y0aHbs055a8YP3cP8lVNSu8kHaYx9dHLoplN00Erj1dnuPUGrq5-r5a_05vb69_LHTVpDwSBtSgqMcUIo5RLqpoCKFbjKIG9rXJU0p5xXNea5LGPR5A0oXlHVtk2FW5bBCfq-1cYt_4zKB7HWvlbGyF7Z0YssoyzHFMoZ_fYP-mRH18flRAaQxaBZTiN1vqVqZ713qhWD02vpJkGwmK8h5jzExzUi_HWnHKu1av6i-_gjQLbARhs1_Ucl7u5vV1vpO4V9m7k</recordid><startdate>202002</startdate><enddate>202002</enddate><creator>Hanazono, Yuya</creator><creator>Takeda, Kazuki</creator><creator>Miki, Kunio</creator><general>John Wiley & Sons, Inc</general><general>Wiley Subscription Services, Inc</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>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4094-6816</orcidid><orcidid>https://orcid.org/0000-0002-3102-2945</orcidid></search><sort><creationdate>202002</creationdate><title>Characterization of perdeuterated high‐potential iron‐sulfur protein with high‐resolution X‐ray crystallography</title><author>Hanazono, Yuya ; Takeda, Kazuki ; Miki, Kunio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3573-d96377811668a3cd53b750b234fc0b964688bc084a988bd4d3e8b6effdb0f723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Chromatiaceae - metabolism</topic><topic>Circular Dichroism</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>Deuterium - chemistry</topic><topic>high resolution</topic><topic>HiPIP</topic><topic>Hydrogen atoms</topic><topic>Hydrogen Bonding</topic><topic>Iron</topic><topic>Iron-Sulfur Proteins - chemistry</topic><topic>iron‐sulfur cluster</topic><topic>Models, Molecular</topic><topic>neutron crystallography</topic><topic>Neutrons</topic><topic>perdeuteration</topic><topic>Photosynthetic Reaction Center Complex Proteins - chemistry</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Sulfur</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hanazono, Yuya</creatorcontrib><creatorcontrib>Takeda, Kazuki</creatorcontrib><creatorcontrib>Miki, Kunio</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</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>Hanazono, Yuya</au><au>Takeda, Kazuki</au><au>Miki, Kunio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of perdeuterated high‐potential iron‐sulfur protein with high‐resolution X‐ray crystallography</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>2020-02</date><risdate>2020</risdate><volume>88</volume><issue>2</issue><spage>251</spage><epage>259</epage><pages>251-259</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high‐resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X‐ray structure of perdeuterated high‐potential iron‐sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high‐resolution neutron crystallography.</abstract><cop>Hoboken, USA</cop><pub>John Wiley & Sons, Inc</pub><pmid>31365157</pmid><doi>10.1002/prot.25793</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-4094-6816</orcidid><orcidid>https://orcid.org/0000-0002-3102-2945</orcidid></addata></record> |
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| subjects | Bacterial Proteins - chemistry Chromatiaceae - metabolism Circular Dichroism Crystallography Crystallography, X-Ray Deuterium - chemistry high resolution HiPIP Hydrogen atoms Hydrogen Bonding Iron Iron-Sulfur Proteins - chemistry iron‐sulfur cluster Models, Molecular neutron crystallography Neutrons perdeuteration Photosynthetic Reaction Center Complex Proteins - chemistry Protein Conformation Proteins Sulfur |
| title | Characterization of perdeuterated high‐potential iron‐sulfur protein with high‐resolution X‐ray crystallography |
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