About: Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough)

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About: Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 1992

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1992 (uk) im Oktober 1992 veröffentlichter wissenschaftlicher Artikel (de) article scientifique publié en 1992 (fr) artículu científicu espublizáu n'ochobre de 1992 (ast) scientific article published on 01 October 1992 (en)
publication date	wds:Q63953778-6EE8556D-A664-480A-B1C1-B6A6B6D32B80
publication date	1992-10-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q63953778-1342827D-6B0E-4A60-A38B-15E1FFC15FC2 wds:Q63953778-1D4E22AC-2BF0-462E-B26C-2CC9B9A9BB14 wds:Q63953778-25B26295-9EE3-4FCE-A123-1FA417F1A914 wds:Q63953778-3F16BDFD-AC09-448F-B7B7-8994E0949B07 wds:Q63953778-4FB3F0D3-B0B7-41DF-AA5A-168CD9FC3DC8 wds:Q63953778-5485FA57-2631-4912-9216-228B6B4D49D7 wds:Q63953778-9C8CAAA1-0D13-4706-9A94-E09A8890C13B wds:Q63953778-F3E4C7E3-61C9-4918-98CC-63A767CDBEDF wds:Q63953778-FD3D1BF5-DBAE-43F2-BBA6-3E23193A2BB0
author name string	W R Hagen C Veeger R B Wolbert R H Sands H J Grande J S Redeker M Boersma M F Verhagen P H Mutsaers
rdfs:label	Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) (en) Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (nl)
skos:prefLabel	Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) (en) Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (nl)
name	Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) (en) Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (nl)
author	wds:Q63953778-F0CEE884-2B5C-4B07-B751-B51541E7A16A
author	Antonio J Pierik
title	wds:Q63953778-F1CDF38F-1121-4883-824A-DA1114713EE0
title	Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) (en)
page(s)	wds:Q63953778-C9F8F50B-616C-44A5-AEB6-72620344EBB1
page(s)	63-72
instance of	wds:Q63953778-E2F13C5B-2BA1-41A9-8055-136D5448B187
instance of	scholarly article
main subject	wds:Q63953778-EF3A964E-6271-4A73-A352-4EF04ADC8899
main subject	Desulfovibrio vulgaris
PubMed ID	wds:Q63953778-7F906D2E-FC00-406E-85DA-E05606A26FD8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1396719
PubMed ID	1396719
published in	wds:Q63953778-50F6E46B-F851-4F8E-84FD-36973A3ECAAE
published in	FEBS Journal
issue	wds:Q63953778-EE7FE2F0-D4B5-4D20-AA1D-1739B5B53966
volume	wds:Q63953778-86DCE00A-10C7-4E63-BBCF-A4DAA28D6910
issue	1
volume	209
DOI	wds:Q63953778-3721A2F9-888E-4F81-A65A-11D0AB960466
DOI	http://dx.doi.org/10.1111/J.1432-1033.1992.TB17261.X
DOI	10.1111/J.1432-1033.1992.TB17261.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q63953778
is cites work of	Chlorite dismutases - a heme enzyme family for use in bioremediation and generation of molecular oxygen. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins Enzymes of hydrogen metabolism in Pyrococcus furiosus Maturation of hydrogenases H2 conversion in the presence of O2 as performed by the membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha Carbon Monoxide and Cyanide as Intrinsic Ligands to Iron in the Active Site of [NiFe]-Hydrogenases The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. I. Light sensitivity and magnetic hyperfine interactions as observed by electron paramagnetic resonance. Spectroscopic characterization and ligand-binding properties of chlorite dismutase from the chlorate respiring bacterial strain GR-1. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center Bovine-heart NADH:ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups. Purification and characterization of the tungsten enzyme aldehyde:ferredoxin oxidoreductase from the hyperthermophilic denitrifier Pyrobaculum aerophilum. The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization. Residue Mutations in [Fe-Fe]-hydrogenase Impedes O(2) Binding: A QM/MM Investigation Inactivation of [Fe-Fe]-Hydrogenase by O(2). Thermodynamics and Frontier Molecular Orbitals Analyses On the two iron centers of desulfoferrodoxin The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy. Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus. Carboxy-terminal processing of the large subunit of [Fe] hydrogenase from Desulfovibrio desulfuricans ATCC 7757 Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing Bacteria Pyrococcus furiosus glyceraldehyde 3-phosphate oxidoreductase has comparable W(6+/5+) and W(5+/4+) reduction potentials and unusual [4Fe-4S] EPR properties Hyperthermophilic redox chemistry: a re-evaluation Redox properties of the sulfhydrogenase from Pyrococcus furiosus Fe-only hydrogenase from Thermotoga maritima A comparative picosecond-resolved fluorescence study of tryptophan residues in iron-sulfur proteins Effects of thiols and mercurials on the periplasmic hydrogenase from Desulfovibrio vulgaris (Hildenborough). Probing the effects of one-electron reduction and protonation on the electronic properties of the Fe-S clusters in the active-ready form of [FeFe]-hydrogenases. A QM/MM investigation Production of a biomimetic Fe(I)-S phase on pyrite by atomic hydrogen beam surface reactive scattering [Fe-Fe]-hydrogenase Reactivated by Residue Mutations as Bridging Carbonyl Rearranges: A QM/MM Study In vitro and in vivo coupling of Thiocapsa hydrogenase with cyanobacterial and algal electron mediators. EPR monitored redox titration of the cofactors of Saccharomyces cerevisiae Nar1.
is cites work of	wds:Q27937584-7678B1D8-E07A-4387-A7D8-70B69AF72E9C wds:Q36647909-9C8C906F-2588-4F32-B564-33F7745DFF7D wds:Q33859875-8F7DC37B-90A4-4936-AFEC-ED915BE3E3CB wds:Q60446924-9A6DC03E-2C79-41AC-AFB1-6C813DC39ACF wds:Q73223981-210E7FE0-1FC3-468C-B000-96588B573C53 wds:Q71889872-7F27F257-F1AE-4466-B0BA-2D4BDCC9D99D wds:Q27937154-9DAC21CA-25D7-4222-BEE4-F7DF1DD73484 wds:Q42636458-5B44D1FE-751F-42A2-9708-35671BD54BD5 wds:Q63953757-AD0B2542-2B55-4CBD-9202-72CFECF52047 wds:Q72067283-F6333BAF-EFFC-4A0D-A2AF-2E9F035EECD0 wds:Q82507446-F74E8753-7715-486F-B74D-B8C49ED45E63 wds:Q35033366-B4F82DE7-540E-499C-B487-6116168E33BA wds:Q35674131-DA4E2D8C-EFED-4B23-A693-F89AA2BA8FF5

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