Single crystal EXAFS of nitrogenase
Single crystals of the nitrogenase Mo-Fe protein have been examined by polarized x-ray absorption spectroscopy. For different orientations, the Mo-Fe amplitude of the Mo K-edge EXAFS was found to change by a factor of 2.5, whereas the Mo-S component varied by only +- 15%. The orientation dependence...
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Veröffentlicht in: | J. Am. Chem. Soc.; (United States) 1986-03, Vol.108 (5), p.1049-1055 |
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creator | Flank, A. M Weininger, M Mortenson, L. E Cramer, S. P |
description | Single crystals of the nitrogenase Mo-Fe protein have been examined by polarized x-ray absorption spectroscopy. For different orientations, the Mo-Fe amplitude of the Mo K-edge EXAFS was found to change by a factor of 2.5, whereas the Mo-S component varied by only +- 15%. The orientation dependence of the EXAFS spectra has been used to investigate the geometry and orientation of the Mo, Fe, S clusters within the Mo-Fe protein. This represents the first application of single-crystal EXAFS to an enzyme of unknown crystal structure. 38 references, 10 figures, 3 tables. |
doi_str_mv | 10.1021/ja00265a034 |
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M ; Weininger, M ; Mortenson, L. E ; Cramer, S. P</creator><creatorcontrib>Flank, A. M ; Weininger, M ; Mortenson, L. E ; Cramer, S. P ; Exxon Research and Engineering Co., Annandale, NJ</creatorcontrib><description>Single crystals of the nitrogenase Mo-Fe protein have been examined by polarized x-ray absorption spectroscopy. For different orientations, the Mo-Fe amplitude of the Mo K-edge EXAFS was found to change by a factor of 2.5, whereas the Mo-S component varied by only +- 15%. The orientation dependence of the EXAFS spectra has been used to investigate the geometry and orientation of the Mo, Fe, S clusters within the Mo-Fe protein. This represents the first application of single-crystal EXAFS to an enzyme of unknown crystal structure. 38 references, 10 figures, 3 tables.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja00265a034</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>400301 - Organic Chemistry- Chemical & Physicochemical Properties- (-1987) ; Biological and medical sciences ; CRYSTAL STRUCTURE ; Crystalline structure ; CRYSTALS ; DATA ; ELEMENTS ; ENZYMES ; EXPERIMENTAL DATA ; Fundamental and applied biological sciences. Psychology ; INFORMATION ; INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY ; IRON ; METALS ; Molecular biophysics ; MOLYBDENUM ; MONOCRYSTALS ; NITRO-GROUP DEHYDROGENASES ; NITROGENASE ; NONMETALS ; NUMERICAL DATA ; OXIDOREDUCTASES ; SPECTROSCOPY ; Structure in molecular biology ; SULFUR ; TRANSITION ELEMENTS ; X-RAY SPECTROSCOPY</subject><ispartof>J. Am. Chem. 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M</creatorcontrib><creatorcontrib>Weininger, M</creatorcontrib><creatorcontrib>Mortenson, L. E</creatorcontrib><creatorcontrib>Cramer, S. P</creatorcontrib><creatorcontrib>Exxon Research and Engineering Co., Annandale, NJ</creatorcontrib><title>Single crystal EXAFS of nitrogenase</title><title>J. Am. Chem. Soc.; (United States)</title><addtitle>J. Am. Chem. Soc</addtitle><description>Single crystals of the nitrogenase Mo-Fe protein have been examined by polarized x-ray absorption spectroscopy. For different orientations, the Mo-Fe amplitude of the Mo K-edge EXAFS was found to change by a factor of 2.5, whereas the Mo-S component varied by only +- 15%. The orientation dependence of the EXAFS spectra has been used to investigate the geometry and orientation of the Mo, Fe, S clusters within the Mo-Fe protein. This represents the first application of single-crystal EXAFS to an enzyme of unknown crystal structure. 38 references, 10 figures, 3 tables.</description><subject>400301 - Organic Chemistry- Chemical & Physicochemical Properties- (-1987)</subject><subject>Biological and medical sciences</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystalline structure</subject><subject>CRYSTALS</subject><subject>DATA</subject><subject>ELEMENTS</subject><subject>ENZYMES</subject><subject>EXPERIMENTAL DATA</subject><subject>Fundamental and applied biological sciences. 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P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a357t-ca99f45b77823a9094b9de0371400165d246e839d0f844cd184c05628205f5a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>400301 - Organic Chemistry- Chemical & Physicochemical Properties- (-1987)</topic><topic>Biological and medical sciences</topic><topic>CRYSTAL STRUCTURE</topic><topic>Crystalline structure</topic><topic>CRYSTALS</topic><topic>DATA</topic><topic>ELEMENTS</topic><topic>ENZYMES</topic><topic>EXPERIMENTAL DATA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>INFORMATION</topic><topic>INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY</topic><topic>IRON</topic><topic>METALS</topic><topic>Molecular biophysics</topic><topic>MOLYBDENUM</topic><topic>MONOCRYSTALS</topic><topic>NITRO-GROUP DEHYDROGENASES</topic><topic>NITROGENASE</topic><topic>NONMETALS</topic><topic>NUMERICAL DATA</topic><topic>OXIDOREDUCTASES</topic><topic>SPECTROSCOPY</topic><topic>Structure in molecular biology</topic><topic>SULFUR</topic><topic>TRANSITION ELEMENTS</topic><topic>X-RAY SPECTROSCOPY</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Flank, A. M</creatorcontrib><creatorcontrib>Weininger, M</creatorcontrib><creatorcontrib>Mortenson, L. E</creatorcontrib><creatorcontrib>Cramer, S. P</creatorcontrib><creatorcontrib>Exxon Research and Engineering Co., Annandale, NJ</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>OSTI.GOV</collection><jtitle>J. Am. Chem. Soc.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Flank, A. M</au><au>Weininger, M</au><au>Mortenson, L. E</au><au>Cramer, S. P</au><aucorp>Exxon Research and Engineering Co., Annandale, NJ</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Single crystal EXAFS of nitrogenase</atitle><jtitle>J. Am. Chem. Soc.; (United States)</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>1986-03-01</date><risdate>1986</risdate><volume>108</volume><issue>5</issue><spage>1049</spage><epage>1055</epage><pages>1049-1055</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>Single crystals of the nitrogenase Mo-Fe protein have been examined by polarized x-ray absorption spectroscopy. For different orientations, the Mo-Fe amplitude of the Mo K-edge EXAFS was found to change by a factor of 2.5, whereas the Mo-S component varied by only +- 15%. The orientation dependence of the EXAFS spectra has been used to investigate the geometry and orientation of the Mo, Fe, S clusters within the Mo-Fe protein. This represents the first application of single-crystal EXAFS to an enzyme of unknown crystal structure. 38 references, 10 figures, 3 tables.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/ja00265a034</doi><tpages>7</tpages></addata></record> |
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subjects | 400301 - Organic Chemistry- Chemical & Physicochemical Properties- (-1987) Biological and medical sciences CRYSTAL STRUCTURE Crystalline structure CRYSTALS DATA ELEMENTS ENZYMES EXPERIMENTAL DATA Fundamental and applied biological sciences. Psychology INFORMATION INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY IRON METALS Molecular biophysics MOLYBDENUM MONOCRYSTALS NITRO-GROUP DEHYDROGENASES NITROGENASE NONMETALS NUMERICAL DATA OXIDOREDUCTASES SPECTROSCOPY Structure in molecular biology SULFUR TRANSITION ELEMENTS X-RAY SPECTROSCOPY |
title | Single crystal EXAFS of nitrogenase |
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