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Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit

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Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit. / Pinske, Constanze; Krüger, Sara; Soboh, Basem; Ihling, Christian; Kuhns, Martin; Braussemann, Mario; Jaroschinsky, Monique; Sauer, Christopher; Sargent, Frank; Sinz, Andrea; Sawers, R. Gary.

In: Archives of Microbiology, Vol. 193, No. 12, 12.2011, p. 893-903.

Research output: Contribution to journalArticle

Harvard

Pinske, C, Krüger, S, Soboh, B, Ihling, C, Kuhns, M, Braussemann, M, Jaroschinsky, M, Sauer, C, Sargent, F, Sinz, A & Sawers, RG 2011, 'Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit' Archives of Microbiology, vol 193, no. 12, pp. 893-903.

APA

Pinske, C., Krüger, S., Soboh, B., Ihling, C., Kuhns, M., Braussemann, M., Jaroschinsky, M., Sauer, C., Sargent, F., Sinz, A., & Sawers, R. G. (2011). Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit. Archives of Microbiology, 193(12), 893-903doi: 10.1007/s00203-011-0726-5

Vancouver

Pinske C, Krüger S, Soboh B, Ihling C, Kuhns M, Braussemann M et al. Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit. Archives of Microbiology. 2011 Dec;193(12):893-903.

Author

Pinske, Constanze; Krüger, Sara; Soboh, Basem; Ihling, Christian; Kuhns, Martin; Braussemann, Mario; Jaroschinsky, Monique; Sauer, Christopher; Sargent, Frank; Sinz, Andrea; Sawers, R. Gary / Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit.

In: Archives of Microbiology, Vol. 193, No. 12, 12.2011, p. 893-903.

Research output: Contribution to journalArticle

Bibtex - Download

@article{458e988895e24146a43b212ec95c1ea5,
title = "Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit",
author = "Constanze Pinske and Sara Krüger and Basem Soboh and Christian Ihling and Martin Kuhns and Mario Braussemann and Monique Jaroschinsky and Christopher Sauer and Frank Sargent and Andrea Sinz and Sawers, {R. Gary}",
year = "2011",
volume = "193",
number = "12",
pages = "893--903",
journal = "Archives of Microbiology",
issn = "0302-8933",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron-sulfur cluster-containing small subunit

A1 - Pinske,Constanze

A1 - Krüger,Sara

A1 - Soboh,Basem

A1 - Ihling,Christian

A1 - Kuhns,Martin

A1 - Braussemann,Mario

A1 - Jaroschinsky,Monique

A1 - Sauer,Christopher

A1 - Sargent,Frank

A1 - Sinz,Andrea

A1 - Sawers,R. Gary

AU - Pinske,Constanze

AU - Krüger,Sara

AU - Soboh,Basem

AU - Ihling,Christian

AU - Kuhns,Martin

AU - Braussemann,Mario

AU - Jaroschinsky,Monique

AU - Sauer,Christopher

AU - Sargent,Frank

AU - Sinz,Andrea

AU - Sawers,R. Gary

PY - 2011/12

Y1 - 2011/12

N2 - <p>Escherichia coli can both oxidize hydrogen and reduce protons. These activities involve three distinct [NiFe]-hydrogenases, termed Hyd-1, Hyd-2, and Hyd-3, each minimally comprising heterodimers of a large subunit, containing the [NiFe] active site, and a small subunit, bearing iron-sulfur clusters. Dihydrogen-oxidizing activity can be determined using redox dyes like benzyl viologen (BV); however, it is unclear whether electron transfer to BV occurs directly at the active site, or via an iron-sulfur center in the small subunit. Plasmids encoding Strep-tagged derivatives of the large subunits of the three E. coli [NiFe]-hydrogenases restored activity of the respective hydrogenase to strain FTD147, which carries in-frame deletions in the hyaB, hybC, and hycE genes encoding the large subunits of Hyd-1, Hyd-2, and Hyd-3, respectively. Purified Strep-HyaB was associated with the Hyd-1 small subunit (HyaA), and purified Strep-HybC was associated with the Hyd-2 small subunit (HybO), and a second iron-sulfur protein, HybA. However, Strep-HybC isolated from a hybO mutant had no other associated subunits and lacked BV-dependent hydrogenase activity. Mutants deleted separately for hyaA, hybO, or hycG (Hyd-3 small subunit) lacked BV-linked hydrogenase activity, despite the Hyd-1 and Hyd-2 large subunits being processed. These findings demonstrate that hydrogenase-dependent reduction of BV requires the small subunit.</p>

AB - <p>Escherichia coli can both oxidize hydrogen and reduce protons. These activities involve three distinct [NiFe]-hydrogenases, termed Hyd-1, Hyd-2, and Hyd-3, each minimally comprising heterodimers of a large subunit, containing the [NiFe] active site, and a small subunit, bearing iron-sulfur clusters. Dihydrogen-oxidizing activity can be determined using redox dyes like benzyl viologen (BV); however, it is unclear whether electron transfer to BV occurs directly at the active site, or via an iron-sulfur center in the small subunit. Plasmids encoding Strep-tagged derivatives of the large subunits of the three E. coli [NiFe]-hydrogenases restored activity of the respective hydrogenase to strain FTD147, which carries in-frame deletions in the hyaB, hybC, and hycE genes encoding the large subunits of Hyd-1, Hyd-2, and Hyd-3, respectively. Purified Strep-HyaB was associated with the Hyd-1 small subunit (HyaA), and purified Strep-HybC was associated with the Hyd-2 small subunit (HybO), and a second iron-sulfur protein, HybA. However, Strep-HybC isolated from a hybO mutant had no other associated subunits and lacked BV-dependent hydrogenase activity. Mutants deleted separately for hyaA, hybO, or hycG (Hyd-3 small subunit) lacked BV-linked hydrogenase activity, despite the Hyd-1 and Hyd-2 large subunits being processed. These findings demonstrate that hydrogenase-dependent reduction of BV requires the small subunit.</p>

KW - [NiFe]-hydrogenase

KW - Iron-sulfur cluster

KW - Electron transfer

KW - Hydrogen evolution

KW - Hydrogen oxidation

KW - Viologen dyes

KW - MUTATIONAL ANALYSIS

KW - DESULFOVIBRIO-GIGAS

KW - MATURATION

KW - OPERON

KW - PROTEINS

KW - K-12

KW - PURIFICATION

KW - ISOENZYMES

KW - MEMBRANE

KW - STEP

U2 - 10.1007/s00203-011-0726-5

DO - 10.1007/s00203-011-0726-5

M1 - Article

JO - Archives of Microbiology

JF - Archives of Microbiology

SN - 0302-8933

IS - 12

VL - 193

SP - 893

EP - 903

ER -

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