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Solvent Tuning of Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin
A persistent puzzle in the field of biological electron transfer is the conserved iron-sulfur cluster motif in both high potential iron-sulfur protein (HiPIP) and ferredoxin (Fd) active sites. Despite this structural similarity, HiPIPs react oxidatively at physiological potentials, whereas Fds are r...
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| Published in: | Science (American Association for the Advancement of Science) 2007-11, Vol.318 (5855), p.1464-1468 |
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| cites | cdi_FETCH-LOGICAL-c591t-3be3a4cae1d0d5bec2f76af6ecee1396ac4c7be54844b77c6220a928fcbcc44a3 |
| container_end_page | 1468 |
| container_issue | 5855 |
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| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 318 |
| creator | Dey, Abhishek Jenney, Francis E. Jr Adams, Michael W.W Babini, Elena Takahashi, Yasuhiro Fukuyama, Keiichi Hodgson, Keith O Hedman, Britt Solomon, Edward I |
| description | A persistent puzzle in the field of biological electron transfer is the conserved iron-sulfur cluster motif in both high potential iron-sulfur protein (HiPIP) and ferredoxin (Fd) active sites. Despite this structural similarity, HiPIPs react oxidatively at physiological potentials, whereas Fds are reduced. Sulfur K-edge x-ray absorption spectroscopy uncovers the substantial influence of hydration on this variation in reactivity. Fe-S covalency is much lower in natively hydrated Fd active sites than in HiPIPs but increases upon water removal; similarly, HiPIP covalency decreases when unfolding exposes an otherwise hydrophobically shielded active site to water. Studies on model compounds and accompanying density functional theory calculations support a correlation of Fe-S covalency with ease of oxidation and therefore suggest that hydration accounts for most of the difference between Fd and HiPIP reduction potentials. |
| doi_str_mv | 10.1126/science.1147753 |
| format | article |
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Fe-S covalency is much lower in natively hydrated Fd active sites than in HiPIPs but increases upon water removal; similarly, HiPIP covalency decreases when unfolding exposes an otherwise hydrophobically shielded active site to water. Studies on model compounds and accompanying density functional theory calculations support a correlation of Fe-S covalency with ease of oxidation and therefore suggest that hydration accounts for most of the difference between Fd and HiPIP reduction potentials.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1147753</identifier><identifier>PMID: 18048692</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Active sites ; Analytical, structural and metabolic biochemistry ; Bacterial Proteins - chemistry ; Binding Sites ; Biochemistry ; Biological ; Biological and medical sciences ; Biophysics ; Chemical compounds ; Covalence ; Covalent bonds ; Electricity ; Electrochemistry ; Electrode potentials ; Electrostatics ; Ferredoxins ; Ferredoxins - chemistry ; Fundamental and applied biological sciences. Psychology ; Hydration ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Iron ; Iron - chemistry ; Iron-Sulfur Proteins - chemistry ; Ligands ; Metalloproteins ; Molecules ; Orbitals ; Other metalloproteins ; Oxidation ; Oxidation-Reduction ; Photosynthetic Reaction Center Complex Proteins - chemistry ; Protein Folding ; Proteins ; Similarity ; Solvents ; Spectrum Analysis ; Static Electricity ; Sulfur ; Sulfur - chemistry ; Tuning ; Water - chemistry</subject><ispartof>Science (American Association for the Advancement of Science), 2007-11, Vol.318 (5855), p.1464-1468</ispartof><rights>Copyright 2007 American Association for the Advancement of Science</rights><rights>2008 INIST-CNRS</rights><rights>Copyright © 2007, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c591t-3be3a4cae1d0d5bec2f76af6ecee1396ac4c7be54844b77c6220a928fcbcc44a3</citedby><cites>FETCH-LOGICAL-c591t-3be3a4cae1d0d5bec2f76af6ecee1396ac4c7be54844b77c6220a928fcbcc44a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20051713$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20051713$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,2882,2883,27922,27923,58236,58469</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19896982$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18048692$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dey, Abhishek</creatorcontrib><creatorcontrib>Jenney, Francis E. Jr</creatorcontrib><creatorcontrib>Adams, Michael W.W</creatorcontrib><creatorcontrib>Babini, Elena</creatorcontrib><creatorcontrib>Takahashi, Yasuhiro</creatorcontrib><creatorcontrib>Fukuyama, Keiichi</creatorcontrib><creatorcontrib>Hodgson, Keith O</creatorcontrib><creatorcontrib>Hedman, Britt</creatorcontrib><creatorcontrib>Solomon, Edward I</creatorcontrib><title>Solvent Tuning of Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>A persistent puzzle in the field of biological electron transfer is the conserved iron-sulfur cluster motif in both high potential iron-sulfur protein (HiPIP) and ferredoxin (Fd) active sites. Despite this structural similarity, HiPIPs react oxidatively at physiological potentials, whereas Fds are reduced. Sulfur K-edge x-ray absorption spectroscopy uncovers the substantial influence of hydration on this variation in reactivity. Fe-S covalency is much lower in natively hydrated Fd active sites than in HiPIPs but increases upon water removal; similarly, HiPIP covalency decreases when unfolding exposes an otherwise hydrophobically shielded active site to water. Studies on model compounds and accompanying density functional theory calculations support a correlation of Fe-S covalency with ease of oxidation and therefore suggest that hydration accounts for most of the difference between Fd and HiPIP reduction potentials.</description><subject>Active sites</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacterial Proteins - chemistry</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological</subject><subject>Biological and medical sciences</subject><subject>Biophysics</subject><subject>Chemical compounds</subject><subject>Covalence</subject><subject>Covalent bonds</subject><subject>Electricity</subject><subject>Electrochemistry</subject><subject>Electrode potentials</subject><subject>Electrostatics</subject><subject>Ferredoxins</subject><subject>Ferredoxins - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydration</subject><subject>Hydrogen Bonding</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Iron</subject><subject>Iron - chemistry</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>Ligands</subject><subject>Metalloproteins</subject><subject>Molecules</subject><subject>Orbitals</subject><subject>Other metalloproteins</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Photosynthetic Reaction Center Complex Proteins - chemistry</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Similarity</subject><subject>Solvents</subject><subject>Spectrum Analysis</subject><subject>Static Electricity</subject><subject>Sulfur</subject><subject>Sulfur - chemistry</subject><subject>Tuning</subject><subject>Water - chemistry</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqF0U1r3DAQBmBRWprttuee2opCPy5uRh-WrGMISRMIdGGTXnowsnacaPFaqWSH5t9HZk0DPaQnI-aZ1zAvIW8ZfGOMq8PkPPYO80NqXYpnZMHAlIXhIJ6TBYBQRQW6PCCvUtoC5JkRL8kBq0BWyvAF-bUO3R32A70ce99f09DSkw7dEIO7wZ13tqOrMGTgbZeo7-lwg_TIDf4O6doPmKaNM786X9GfGNOY6CnGiJvwx_evyYs2b-Gb-bskV6cnl8dnxcWP7-fHRxeFKw0bCtGgsNJZZBvYlA063mplW4UOkQmjrJNON1jKSspGa6c4B2t41brGOSmtWJIv-9zbGH6PmIZ655PDrrM9hjHVWgpZcoAyy89PSmUANCv_D4XigrN8zCX5-iRkUHFmuOJVph__odswxj5fpuZMKABpeEaHe-RiSCliW99Gv7PxPifVU-X1XHk9V5433s-xY7PDzaOfO87g0wxsyn220fbOp0dnKqNMNbl3e7dNQ4h_59PhmGbTjz7s560Ntb2OOeNqzYEJgEpI0EY8AKGsx1k</recordid><startdate>20071130</startdate><enddate>20071130</enddate><creator>Dey, Abhishek</creator><creator>Jenney, Francis E. 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Psychology</topic><topic>Hydration</topic><topic>Hydrogen Bonding</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Iron</topic><topic>Iron - chemistry</topic><topic>Iron-Sulfur Proteins - chemistry</topic><topic>Ligands</topic><topic>Metalloproteins</topic><topic>Molecules</topic><topic>Orbitals</topic><topic>Other metalloproteins</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Photosynthetic Reaction Center Complex Proteins - chemistry</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Similarity</topic><topic>Solvents</topic><topic>Spectrum Analysis</topic><topic>Static Electricity</topic><topic>Sulfur</topic><topic>Sulfur - chemistry</topic><topic>Tuning</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dey, Abhishek</creatorcontrib><creatorcontrib>Jenney, Francis E. 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Jr</au><au>Adams, Michael W.W</au><au>Babini, Elena</au><au>Takahashi, Yasuhiro</au><au>Fukuyama, Keiichi</au><au>Hodgson, Keith O</au><au>Hedman, Britt</au><au>Solomon, Edward I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solvent Tuning of Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2007-11-30</date><risdate>2007</risdate><volume>318</volume><issue>5855</issue><spage>1464</spage><epage>1468</epage><pages>1464-1468</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>A persistent puzzle in the field of biological electron transfer is the conserved iron-sulfur cluster motif in both high potential iron-sulfur protein (HiPIP) and ferredoxin (Fd) active sites. Despite this structural similarity, HiPIPs react oxidatively at physiological potentials, whereas Fds are reduced. Sulfur K-edge x-ray absorption spectroscopy uncovers the substantial influence of hydration on this variation in reactivity. Fe-S covalency is much lower in natively hydrated Fd active sites than in HiPIPs but increases upon water removal; similarly, HiPIP covalency decreases when unfolding exposes an otherwise hydrophobically shielded active site to water. Studies on model compounds and accompanying density functional theory calculations support a correlation of Fe-S covalency with ease of oxidation and therefore suggest that hydration accounts for most of the difference between Fd and HiPIP reduction potentials.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>18048692</pmid><doi>10.1126/science.1147753</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Science (American Association for the Advancement of Science), 2007-11, Vol.318 (5855), p.1464-1468 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743452005 |
| source | American Association for the Advancement of Science; Alma/SFX Local Collection; JSTOR |
| subjects | Active sites Analytical, structural and metabolic biochemistry Bacterial Proteins - chemistry Binding Sites Biochemistry Biological Biological and medical sciences Biophysics Chemical compounds Covalence Covalent bonds Electricity Electrochemistry Electrode potentials Electrostatics Ferredoxins Ferredoxins - chemistry Fundamental and applied biological sciences. Psychology Hydration Hydrogen Bonding Hydrophobic and Hydrophilic Interactions Iron Iron - chemistry Iron-Sulfur Proteins - chemistry Ligands Metalloproteins Molecules Orbitals Other metalloproteins Oxidation Oxidation-Reduction Photosynthetic Reaction Center Complex Proteins - chemistry Protein Folding Proteins Similarity Solvents Spectrum Analysis Static Electricity Sulfur Sulfur - chemistry Tuning Water - chemistry |
| title | Solvent Tuning of Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin |
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