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[[Image: | ==Crystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenase== | ||
<StructureSection load='1wzd' size='340' side='right' caption='[[1wzd]], [[Resolution|resolution]] 1.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1wzd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZD FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOK:[[2,2-[4-CARBOXYETHYL-1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOK</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iw0|1iw0]], [[1iw1|1iw1]], [[1v8x|1v8x]], [[1wzf|1wzf]], [[1wzg|1wzg]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wzd RCSB], [http://www.ebi.ac.uk/pdbsum/1wzd PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/1wzd_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein-to-protein electron transfer (ET) is a critical process in biological chemistry for which fundamental understanding is expected to provide a wealth of applications in biotechnology. Investigations of protein-protein ET systems in reductive activation of artificial cofactors introduced into proteins remains particularly challenging because of the complexity of interactions between the cofactor and the system contributing to ET. In this work, we construct an artificial protein-protein ET system, using heme oxygenase (HO), which is known to catalyze the conversion of heme to biliverdin. HO uses electrons provided from NADPH/cytochrome P450 reductase (CPR) through protein-protein complex formation during the enzymatic reaction. We report that a Fe(III)(Schiff-base), in the place of the active-site heme prosthetic group of HO, can be reduced by NADPH/CPR. The crystal structure of the Fe(10-CH(2)CH(2)COOH-Schiff-base).HO composite indicates the presence of a hydrogen bond between the propionic acid carboxyl group and Arg-177 of HO. Furthermore, the ET rate from NADPH/CPR to the composite is 3.5-fold faster than that of Fe(Schiff-base).HO, although the redox potential of Fe(10-CH(2)CH(2)COOH-Schiff-base).HO (-79 mV vs. NHE) is lower than that of Fe(Schiff-base).HO (+15 mV vs. NHE), where NHE is normal hydrogen electrode. This work describes a synthetic metal complex activated by means of a protein-protein ET system, which has not previously been reported. Moreover, the result suggests the importance of the hydrogen bond for the ET reaction of HO. Our Fe(Schiff-base).HO composite model system may provide insights with regard to design of ET biosystems for sensors, catalysts, and electronics devices. | |||
Design of metal cofactors activated by a protein-protein electron transfer system.,Ueno T, Yokoi N, Unno M, Matsui T, Tokita Y, Yamada M, Ikeda-Saito M, Nakajima H, Watanabe Y Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9416-21. Epub 2006 Jun 12. PMID:16769893<ref>PMID:16769893</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Heme oxygenase|Heme oxygenase]] | *[[Heme oxygenase|Heme oxygenase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Corynebacterium diphtheriae]] | [[Category: Corynebacterium diphtheriae]] | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
Revision as of 01:18, 29 September 2014
Crystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenaseCrystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenase
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein-to-protein electron transfer (ET) is a critical process in biological chemistry for which fundamental understanding is expected to provide a wealth of applications in biotechnology. Investigations of protein-protein ET systems in reductive activation of artificial cofactors introduced into proteins remains particularly challenging because of the complexity of interactions between the cofactor and the system contributing to ET. In this work, we construct an artificial protein-protein ET system, using heme oxygenase (HO), which is known to catalyze the conversion of heme to biliverdin. HO uses electrons provided from NADPH/cytochrome P450 reductase (CPR) through protein-protein complex formation during the enzymatic reaction. We report that a Fe(III)(Schiff-base), in the place of the active-site heme prosthetic group of HO, can be reduced by NADPH/CPR. The crystal structure of the Fe(10-CH(2)CH(2)COOH-Schiff-base).HO composite indicates the presence of a hydrogen bond between the propionic acid carboxyl group and Arg-177 of HO. Furthermore, the ET rate from NADPH/CPR to the composite is 3.5-fold faster than that of Fe(Schiff-base).HO, although the redox potential of Fe(10-CH(2)CH(2)COOH-Schiff-base).HO (-79 mV vs. NHE) is lower than that of Fe(Schiff-base).HO (+15 mV vs. NHE), where NHE is normal hydrogen electrode. This work describes a synthetic metal complex activated by means of a protein-protein ET system, which has not previously been reported. Moreover, the result suggests the importance of the hydrogen bond for the ET reaction of HO. Our Fe(Schiff-base).HO composite model system may provide insights with regard to design of ET biosystems for sensors, catalysts, and electronics devices. Design of metal cofactors activated by a protein-protein electron transfer system.,Ueno T, Yokoi N, Unno M, Matsui T, Tokita Y, Yamada M, Ikeda-Saito M, Nakajima H, Watanabe Y Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9416-21. Epub 2006 Jun 12. PMID:16769893[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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