Výsledky vyhledávání - "Gary, Sawers"

Akademický článek

Evidence the Isc iron–sulfur cluster biogenesis machinery is the source of iron for [NiFe]-cofactor biosynthesis in Escherichia coli

Autor: Alexander Haase, Christian Arlt, Andrea Sinz, R. Gary Sawers

Publikováno v: Scientific Reports, Vol 14, Iss 1, Pp 1-13 (2024)

Abstract [NiFe]-hydrogenases have a bimetallic NiFe(CN)2CO cofactor in their large, catalytic subunit. The 136 Da Fe(CN)2CO group of this cofactor is preassembled on a distinct HypC–HypD scaffold complex, but the intracellular source of the iron io

Externí odkaz: https://doaj.org/article/b38044cbc381492b8e8d0814985edc7e

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Akademický článek

A redox‐active HybG‐HypD scaffold complex is required for optimal ATPase activity during [NiFe]‐hydrogenase maturation in Escherichia coli

Autor: Alexander Haase, R. Gary Sawers

Publikováno v: FEBS Open Bio, Vol 13, Iss 2, Pp 341-351 (2023)

Four Hyp proteins build a scaffold complex upon which the Fe(CN)2CO group of the [NiFe]‐cofactor of hydrogenases (Hyd) is made. Two of these Hyp proteins, the redox‐active, [4Fe‐4S]‐containing HypD protein and the HypC chaperone, form the bas

Externí odkaz: https://doaj.org/article/e6591069e3b747df8625910188b763e4

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Akademický článek

Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)2CO group during maturation of E. coli [NiFe]-hydrogenase 2

Autor: Christian Arlt, Kerstin Nutschan, Alexander Haase, Christian Ihling, Dirk Tänzler, Andrea Sinz, R. Gary Sawers

Publikováno v: Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)

Abstract [NiFe]-hydrogenases activate dihydrogen. Like all [NiFe]-hydrogenases, hydrogenase 2 of Escherichia coli has a bimetallic NiFe(CN)2CO cofactor in its catalytic subunit. Biosynthesis of the Fe(CN)2CO group of the [NiFe]-cofactor occurs on a d

Externí odkaz: https://doaj.org/article/6b317772a56a40de866920a3a8b490f6

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Akademický článek

Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel

Autor: Michelle Kammel, R. Gary Sawers

Publikováno v: MicrobiologyOpen, Vol 11, Iss 4, Pp n/a-n/a (2022)

Abstract The formate‐specific anion channel FocA of Escherichia coli belongs to the superfamily of homopentameric formate‐nitrite transporters (FNT). Minimally nine amino acid residues are conserved in the formate translocation pore of each proto

Externí odkaz: https://doaj.org/article/2b3f9c7fc6bf444fbfc165a2e702cd79

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Akademický článek

Co‐purification of nitrate reductase 1 with components of the cytochrome bcc‐aa3 oxidase supercomplex from spores of Streptomyces coelicolor A3(2)

Autor: Dörte Falke, Marco Fischer, Christian Ihling, Claudia Hammerschmidt, Andrea Sinz, Gary Sawers

Publikováno v: FEBS Open Bio, Vol 11, Iss 3, Pp 652-669 (2021)

In order to reduce nitrate in vivo, the spore‐specific respiratory nitrate reductase, Nar1, of Streptomyces coelicolor relies on an active cytochrome bcc‐aa3 oxidase supercomplex (bcc‐aa3 supercomplex). This suggests that membrane‐associated

Externí odkaz: https://doaj.org/article/6c44bb6bb60045cebb70ffc6b561c854

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Akademický článek

Coordinated Expression of the Genes Encoding FocA and Pyruvate Formate-Lyase Is Important for Maintenance of Formate Homeostasis during Fermentative Growth of Escherichia coli

Autor: Michelle Kammel, Robert Gary Sawers

Publikováno v: Fermentation, Vol 9, Iss 4, p 382 (2023)

FocA is a pentameric membrane channel that translocates formic acid bidirectionally across the cytoplasmic membrane of Escherichia coli during fermentation. The focA gene is co-transcribed with pflB, which encodes pyruvate formate-lyase, the enzyme t

Externí odkaz: https://doaj.org/article/b5578a9019954f31b06686443b25501e

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Akademický článek

Exchange of a Single Amino Acid Residue in the HybG Chaperone Allows Maturation of All H2-Activating [NiFe]-Hydrogenases in Escherichia coli

Autor: Alexander Haase, R. Gary Sawers

Publikováno v: Frontiers in Microbiology, Vol 13 (2022)

The biosynthesis of the NiFe(CN)2CO organometallic cofactor of [NiFe]-hydrogenase (Hyd) involves several discreet steps, including the synthesis of the Fe(CN)2CO group on a HypD-HypC scaffold complex. HypC has an additional function in transferring t

Externí odkaz: https://doaj.org/article/6acfd093cf9542e2a4e04e83d23fbb22

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Akademický článek

The iron–sulfur‐containing HypC‐HypD scaffold complex of the [NiFe]‐hydrogenase maturation machinery is an ATPase

Autor: Kerstin Nutschan, Ralph P. Golbik, R. Gary Sawers

Publikováno v: FEBS Open Bio, Vol 9, Iss 12, Pp 2072-2079 (2019)

HypD and HypC, or its paralogue HybG in Escherichia coli, form the core of the scaffold complex that synthesizes the Fe(CN)2CO component of the bimetallic NiFe‐cofactor of [NiFe]‐hydrogenase. We show here that purified HypC‐HypD and HybG‐HypD

Externí odkaz: https://doaj.org/article/b317abb622554ddb9e9ca3f6b2ee293d

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Akademický článek

Delimiting the Function of the C-Terminal Extension of the Escherichia coli [NiFe]-Hydrogenase 2 Large Subunit Precursor

Autor: Constanze Pinske, Claudia Thomas, Kerstin Nutschan, R. Gary Sawers

Publikováno v: Frontiers in Microbiology, Vol 10 (2019)

The active site of all [NiFe]-hydrogenases (Hyd) has a bimetallic NiFe(CN)2CO cofactor that requires the combined action of several maturation proteins for its biosynthesis and insertion into the precursor form of the large subunit of the enzyme. Cof

Externí odkaz: https://doaj.org/article/0301dca571af4a618613aed6e7d0682c

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