8doi - Revision history

OCA at 15:04, 13 August 2026

2026-08-13T15:04:00Z

← Older revision		Revision as of 15:04, 13 August 2026
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/Q9NAV7_9ANNE Q9NAV7_9ANNE]		[https://www.uniprot.org/uniprot/Q9NAV7_9ANNE Q9NAV7_9ANNE]
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Dehaloperoxidase (DHP) from the marine polychaete Amphitrite ornata is a multifunctional enzyme that possesses peroxidase, peroxygenase, oxidase and oxygenase activities. Herein, we investigated the reactivity of DHP B with bisphenol A (BPA) and related compounds (bisphenol E, bisphenol F, tetrachlorobisphenol A, 2,2'-biphenol, 3,3'-biphenol, 4,4'-biphenol, and 3,3'-dibromo-4,4'-biphenol). As a previously unknown substrate for DHP B, BPA (as a representative substrate) is an endocrine disruptor widely used in polycarbonate and epoxy resins, thus resulting in human exposure. Reactivity studies with these substrates were investigated using high performance liquid chromatography (HPLC), and their corresponding oxidation products were determined by mass spectrometry (GC-MS/ LC-MS). BPA undergoes oxidation in the presence of DHP B and hydrogen peroxide yielding two cleavage products (4-isopropenylphenol and 4-(2-hydroxypropan-2-yl)phenol), and oligomers with varying degrees of oxidation. (18)O-labeling studies confirmed that the O-atom incorporated into the products was derived exclusively from water, consistent with substrate oxidation via a peroxidase-based mechanism. The X-ray crystal structures of DHP bound with bisphenol E (1.48 A), bisphenol F (1.75 A), 2,2'-biphenol (1.90 A) and 3,3'-biphenol (1.30 A) showed substrate binding sites are in the distal pocket of the heme cofactor, similar to other previously studied DHP substrates. Stopped-flow UV-visible spectroscopy was utilized to investigate the mechanistic details and enzyme oxidation states during substrate turnover, and a reaction mechanism is proposed. The data presented here strongly suggest that DHP B can catalyze the oxidation of bisphenols and biphenols, thus providing evidence of how infaunal invertebrates can contribute to the biotransformation of these marine pollutants.

	Oxidation of bisphenol A (BPA) and related compounds by the multifunctional catalytic globin dehaloperoxidase.,Yun D, de Serrano V, Ghiladi RA J Inorg Biochem. 2022 Oct 6:112020. doi: 10.1016/j.jinorgbio.2022.112020. PMID:36272837<ref>PMID:36272837</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 8doi" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Dehaloperoxidase 3D structures\|Dehaloperoxidase 3D structures]]		*[[Dehaloperoxidase 3D structures\|Dehaloperoxidase 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:12, 25 October 2023

2023-10-25T10:12:02Z

← Older revision		Revision as of 10:12, 25 October 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8doi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amphitrite_ornata Amphitrite ornata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DOI FirstGlance]. <br>		<table><tr><td colspan='2'>[[8doi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amphitrite_ornata Amphitrite ornata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DOI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5VL:2-(2-HYDROXYPHENYL)PHENOL'>5VL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.93Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5VL:2-(2-HYDROXYPHENYL)PHENOL'>5VL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8doi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8doi OCA], [https://pdbe.org/8doi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8doi RCSB], [https://www.ebi.ac.uk/pdbsum/8doi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8doi ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8doi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8doi OCA], [https://pdbe.org/8doi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8doi RCSB], [https://www.ebi.ac.uk/pdbsum/8doi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8doi ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 8doi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 8doi" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Dehaloperoxidase 3D structures\|Dehaloperoxidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:25, 3 November 2022

2022-11-03T07:25:22Z

← Older revision		Revision as of 07:25, 3 November 2022
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 8doi is ~~ON HOLD until Paper~~ Publication		==Dehaloperoxidase B in complex with 2,2'-Biphenol==
			<StructureSection load='8doi' size='340' side='right'caption='[[8doi]], [[Resolution\|resolution]] 1.93Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[8doi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amphitrite_ornata Amphitrite ornata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DOI FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5VL:2-(2-HYDROXYPHENYL)PHENOL'>5VL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8doi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8doi OCA], [https://pdbe.org/8doi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8doi RCSB], [https://www.ebi.ac.uk/pdbsum/8doi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8doi ProSAT]</span></td></tr>
			</table>
			== Function ==
			[https://www.uniprot.org/uniprot/Q9NAV7_9ANNE Q9NAV7_9ANNE]
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Dehaloperoxidase (DHP) from the marine polychaete Amphitrite ornata is a multifunctional enzyme that possesses peroxidase, peroxygenase, oxidase and oxygenase activities. Herein, we investigated the reactivity of DHP B with bisphenol A (BPA) and related compounds (bisphenol E, bisphenol F, tetrachlorobisphenol A, 2,2'-biphenol, 3,3'-biphenol, 4,4'-biphenol, and 3,3'-dibromo-4,4'-biphenol). As a previously unknown substrate for DHP B, BPA (as a representative substrate) is an endocrine disruptor widely used in polycarbonate and epoxy resins, thus resulting in human exposure. Reactivity studies with these substrates were investigated using high performance liquid chromatography (HPLC), and their corresponding oxidation products were determined by mass spectrometry (GC-MS/ LC-MS). BPA undergoes oxidation in the presence of DHP B and hydrogen peroxide yielding two cleavage products (4-isopropenylphenol and 4-(2-hydroxypropan-2-yl)phenol), and oligomers with varying degrees of oxidation. (18)O-labeling studies confirmed that the O-atom incorporated into the products was derived exclusively from water, consistent with substrate oxidation via a peroxidase-based mechanism. The X-ray crystal structures of DHP bound with bisphenol E (1.48 A), bisphenol F (1.75 A), 2,2'-biphenol (1.90 A) and 3,3'-biphenol (1.30 A) showed substrate binding sites are in the distal pocket of the heme cofactor, similar to other previously studied DHP substrates. Stopped-flow UV-visible spectroscopy was utilized to investigate the mechanistic details and enzyme oxidation states during substrate turnover, and a reaction mechanism is proposed. The data presented here strongly suggest that DHP B can catalyze the oxidation of bisphenols and biphenols, thus providing evidence of how infaunal invertebrates can contribute to the biotransformation of these marine pollutants.

	~~Authors:~~ de Serrano, V.S.~~, Yun, D~~.~~, Ghiladi, R~~.		Oxidation of bisphenol A (BPA) and related compounds by the multifunctional catalytic globin dehaloperoxidase.,Yun D, de Serrano V, Ghiladi RA J Inorg Biochem. 2022 Oct 6:112020. doi: 10.1016/j.jinorgbio.2022.112020. PMID:36272837<ref>PMID:36272837</ref>

	~~Description: Dehaloperoxidase B in complex with 2~~,~~2''~~-~~Biphenol~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased~~ Structures]]		</div>
	[[Category: ~~De Serrano, V.S~~]]		<div class="pdbe-citations 8doi" style="background-color:#fffaf0;"></div>
	[[Category: Yun, D]]		== References ==
	[[Category: ~~Ghiladi, R~~]]		<references/>
			__TOC__
			</StructureSection>
			[[Category: Amphitrite ornata]]
			[[Category: Large Structures]]
			[[Category: Ghiladi R]]
			[[Category: Yun D]]
			[[Category: De Serrano VS]]

OCA at 05:31, 31 August 2022

2022-08-31T05:31:07Z

← Older revision		Revision as of 05:31, 31 August 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8doi is ON HOLD		The entry 8doi is ON HOLD until Paper Publication

	Authors: de Serrano, V.S., Yun, D., Ghiladi, R.		Authors: de Serrano, V.S., Yun, D., Ghiladi, R.

OCA: Protected "8doi" [edit=sysop:move=sysop]

2022-07-20T04:35:54Z

Protected "8doi" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:35, 20 July 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8doi is ON HOLD Authors: de Serrano, V.S., Yun, D., Ghiladi, R. Description: Dehaloperoxidase B in complex with 2,2''-Biphenol [[Category: Unreleas...

2022-07-20T04:35:52Z

New page: '''Unreleased structure''' The entry 8doi is ON HOLD Authors: de Serrano, V.S., Yun, D., Ghiladi, R. Description: Dehaloperoxidase B in complex with 2,2''-Biphenol [[Category: Unreleas...

New page

'''Unreleased structure'''

The entry 8doi is ON HOLD

Authors: de Serrano, V.S., Yun, D., Ghiladi, R.

Description: Dehaloperoxidase B in complex with 2,2''-Biphenol
[[Category: Unreleased Structures]]
[[Category: De Serrano, V.S]]
[[Category: Yun, D]]
[[Category: Ghiladi, R]]