PMID:2674654 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:44:53Z

change PMID template to TableEdit version

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	'''~~No author listed~~''' (1989) Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer. ''Mol. Gen. Genet.'' '''218''':249-56		'''Blasco, F, Iobbi, C, Giordano, G, Chippaux, M and Bonnefoy, V''' (1989) Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer. ''Mol. Gen. Genet.'' '''218''':249-56
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	!align=left \|Abstract		!align=left \|Abstract

imported>Wikientrybot: replace GO_table_reference with annotationlinks

2013-09-01T19:19:38Z

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imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T19:19:38Z

change PMID template to TableEdit version

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	~~<span style~~ = '~~font-size: large~~'> '~~''Blasco, F, Iobbi, C, Giordano, G, Chippaux, M and Bonnefoy, V~~''' (1989) Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer.''Mol. Gen. Genet.'' '''218''':249-56</~~span>~~		\|-
			!align=left \|Citation
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			'''No author listed''' (1989) Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer. ''Mol. Gen. Genet.'' '''218''':249-56
			\|-
			!align=left \|Abstract
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			The nucleotide sequence of the narGHJI operon that encodes the nitrate reductase of Escherichia coli was completed. It encodes four polypeptides NarG, NarH, NarJ and NarI of molecular weight 138.7, 57.7, 26.5 and 25.5 kDa, respectively. The analysis of deduced amino acid sequence failed to reveal any structure capable of binding iron within the NarG polypeptide. In contrast, cysteine arrangements typical of iron-sulfur centers were found in the NarH polypeptide. This suggested that the latter is an electron transfer unit of the nitrate reductase complex. Such a view is opposite to the current description of the nitrate reductase. The findings allowed us to propose a model for the electron transfer steps that occur during nitrate reduction. The NarG polypeptide was found to display a high degree of homology with numerous E. coli molybdoproteins. Moreover, the same genetic and functional organizations as well as the presence of highly conserved stretches of amino acids were noted between both NarG/NarH and DmsA/DmsB (encoding the dimethyl sulfoxide reductase) pairs.
			\|-
			!align=left \|Links
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			[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2674654 PubMed]

	~~{\|{{Prettytable}} align = 'center' width= '70%'~~
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	\|~~{{TableHeadingColor}}~~ \|~~'''Abstract'''~~ \|~~\| The nucleotide sequence of the narGHJI operon that encodes the nitrate reductase of~~ Escherichia coli was completed. It encodes four polypeptides NarG, NarH, NarJ and NarI of molecular weight 138.7, 57.7, 26.5 and 25.5 kDa, respectively. The analysis of deduced amino acid sequence failed to reveal any structure capable of binding iron within the NarG polypeptide. In contrast, cysteine arrangements typical of iron-sulfur centers were found in the NarH polypeptide. This suggested that the latter is an electron transfer unit of the nitrate reductase complex. Such a view is opposite to the current description of the nitrate reductase. The findings allowed us to propose a model for the electron transfer steps that occur during nitrate reduction. The NarG polypeptide was found to display a high degree of homology with numerous E. coli ~~molybdoproteins. Moreover, the same genetic and functional organizations as well as the presence of highly conserved stretches of amino acids were noted between both NarG~~/~~NarH and DmsA~~/~~DmsB (encoding the dimethyl sulfoxide reductase) pairs.~~		!align=left \|Keywords
	~~</noinclude>~~		\|\|
	\|-		Amino Acid Sequence; Base Sequence; Chromosome Deletion; Cloning, Molecular; Codon; DNA, Bacterial; Electron Transport; Escherichia coli/enzymology; Escherichia coli/genetics; Iron/metabolism; Molecular Sequence Data; Nitrate Reductases/genetics; Operon; Oxidation-Reduction; Protein Binding; Restriction Mapping; Sequence Homology, Nucleic Acid; Software
	\|{{~~TableHeadingColor~~}} ~~nowrap \|'''Links''' \|\| [http~~:~~//www~~.~~ncbi~~.~~nlm.nih.gov/entrez/query.fcgi?cmd~~=~~Retrieve~~&db=~~pubmed~~&~~dopt~~=~~Abstract~~&~~list_uids~~=~~2674654 PubMed~~]
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			<!--box uid=d41d8cd98f00b204e9800998ecf8427e.129378.R52239349f03fe-->
	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}

127.0.0.1: /Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

2010-06-17T20:51:01Z

/Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

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	!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

127.0.0.1: Update TableEdit tables.

2010-01-09T04:40:48Z

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imported>Wikientrybot: Fix links due to TableEditLinks.php changes.

2009-02-20T04:56:35Z

Fix links due to TableEditLinks.php changes.

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	!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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127.0.0.1: Edited by wikibot

2008-04-30T13:01:44Z

Edited by wikibot

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Pei at 10:13, 30 April 2008

2008-04-30T10:13:54Z

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127.0.0.1: Edited by wikibot

2008-04-25T22:41:27Z

Edited by wikibot

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	\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2674654 PubMed]		\|{{TableHeadingColor}} nowrap \|'''Links''' \|\| [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2674654 PubMed]
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}
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	==Annotations {{HelpIcon\|Help:Literature}}==		==Annotations {{HelpIcon\|Help:Literature}}==
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	==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==		==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==

74.192.221.37: New PMID: Page!

2008-02-07T16:16:25Z

New PMID: Page!

New page

<protect>
{{RightTOC}}

<span style = 'font-size: large'> '''Blasco, F, Iobbi, C, Giordano, G, Chippaux, M and Bonnefoy, V''' (1989) Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer.''Mol. Gen. Genet.'' '''218''':249-56</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The nucleotide sequence of the narGHJI operon that encodes the nitrate reductase of Escherichia coli was completed. It encodes four polypeptides NarG, NarH, NarJ and NarI of molecular weight 138.7, 57.7, 26.5 and 25.5 kDa, respectively. The analysis of deduced amino acid sequence failed to reveal any structure capable of binding iron within the NarG polypeptide. In contrast, cysteine arrangements typical of iron-sulfur centers were found in the NarH polypeptide. This suggested that the latter is an electron transfer unit of the nitrate reductase complex. Such a view is opposite to the current description of the nitrate reductase. The findings allowed us to propose a model for the electron transfer steps that occur during nitrate reduction. The NarG polypeptide was found to display a high degree of homology with numerous E. coli molybdoproteins. Moreover, the same genetic and functional organizations as well as the presence of highly conserved stretches of amino acids were noted between both NarG/NarH and DmsA/DmsB (encoding the dimethyl sulfoxide reductase) pairs.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2674654 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='237202'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>