In the facultative sulphate/nitrate reducer Desulfovibrio desulfuricans ATCC 27774, the nine-haem cytochrome c is part of a membrane-bound redox complex mainly expressed in sulphate-grown cells (Q62029913)

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scientific article published in July 2001

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English	In the facultative sulphate/nitrate reducer Desulfovibrio desulfuricans ATCC 27774, the nine-haem cytochrome c is part of a membrane-bound redox complex mainly expressed in sulphate-grown cells	scientific article published in July 2001

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9 November 2019

In the facultative sulphate/nitrate reducer Desulfovibrio desulfuricans ATCC 27774, the nine-haem cytochrome c is part of a membrane-bound redox complex mainly expressed in sulphate-grown cells (English)

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9 November 2019

Desulfovibrio desulfuricans

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Desulfovibrio desulfuricans

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Lígia M. Saraiva

1

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9 November 2019

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P N da Costa

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9 November 2019

C Conte

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9 November 2019

A V Xavier

4

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9 November 2019

J LeGall

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9 November 2019

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1 July 2001

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9 November 2019

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8

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Biochimica et Biophysica Acta

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1520

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9 November 2019

1

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9 November 2019

63-70

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9 November 2019

Cytochrome components of nitrate- and sulfate-respiring Desulfovibrio desulfuricans ATCC 27774.

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Nitrite reductase from Desulfovibrio desulfuricans (ATCC 27774)--a heterooligomer heme protein with sulfite reductase activity

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Characterization of a heme c nitrite reductase from a non-ammonifying microorganism, Desulfovibrio vulgaris Hildenborough

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The primary and three-dimensional structures of a nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc family

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7 January 2021

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Nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774 : primary sequence determination, crystallographic refinement at 1.8 and modelling studies of its interaction with the tetrahaem cytochrome c 3

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[NiFe] hydrogenase from Desulfovibrio desulfuricans ATCC 27774: gene sequencing, three-dimensional structure determination and refinement at 1.8 A and modelling studies of its interaction with the tetrahaem cytochrome c3

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Nonaheme cytochrome c, a new physiological electron acceptor for [Ni,Fe] hydrogenase in the sulfate-reducing bacterium Desulfovibrio desulfuricans Essex: primary sequence, molecular parameters, and redox properties.

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Biochemical and spectroscopic characterization of the high molecular weight cytochrome c from Desulfovibrio vulgaris Hildenborough expressed in Desulfovibrio desulfuricans G200

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Characterization and redox properties of high molecular mass cytochrome c3 (Hmc) isolated from Desulfovibrio vulgaris Miyazaki

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Isolation and characterization of a high molecular weight cytochrome from the sulfate reducing bacterium Desulfovibrio gigas

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The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex

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Sequencing the gene encoding desulfovibrio desulfuricans ATCC 27774 nine-heme cytochrome c.

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Multiple sequence alignment with hierarchical clustering

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A common export pathway for proteins binding complex redox cofactors?

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Cloning, sequencing, and mutational analysis of the hyb operon encoding Escherichia coli hydrogenase 2.

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A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria.

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Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop

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Codon usage tabulated from international DNA sequence databases: status for the year 2000

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Evidence for the presence of a b-type cytochrome in the sulfate-reducing bacterium Desulfovibrio gigas, and its role in the reduction of fumarate by molecular hydrogen

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Localization of dehydrogenases, reductases, and electron transfer components in the sulfate-reducing bacterium Desulfovibrio gigas

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Deletion of two downstream genes alters expression of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough

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Identifiers

10.1016/S0167-4781(01)00250-0

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11470160%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11470160%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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