A Sulfurtransferase Is Essential for Activity of Formate Dehydrogenases in Escherichia coli

Thomé, Rémi; Gust, Alexander; Toci, René; Mendel, Ralf R.; Bittner, Florian; Magalon, Axel; Walburger, Anne

doi:10.1074/jbc.m111.327122

Cited by 75 publications

(106 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Growth conditions for overproduction of EcFdhD and its variants were as in ref. 11. For ICP-MS and FormA-dephospho quantification of Mo-bisPGD, shuffle T7 strain transformed with pET22-FdhD was grown in medium supplemented with Na 2 MoO 4 (1 mM).…”

Section: Methodsmentioning

confidence: 99%

“…This loop is partly disordered in each monomer with residues 113-131 not visible in the electron density map. Remarkably, this disordered part of the loop contains the pair of cysteine residues (Cys121-Cys124) shown to be functionally important 11 . The corresponding loop (residue 89-119) is also disordered in DpFdhD, thereby suggesting a functional role for this disorder ( Supplementary Fig.…”

Section: Ecfdhd Is a Dimer That Binds The Molybdenum Cofactor In Vivomentioning

confidence: 99%

“…The additional sulphur is also found in the Mo coordination sphere of periplasmic nitrate reductases, as well as in members of the xanthine oxidase family 8,9 . Most interestingly, this inorganic sulphur is crucial for the activity of both FDHs and members of the xanthine oxidase family, while its functional significance in periplasmic nitrate reductases remains to be established 10,11 . In Escherichia coli, the FDH activity requires the protein FdhD that was reported to act as a sulphurtransferase between the L-cysteine desulphurase IscS and FDHs 11 .…”

mentioning

confidence: 99%

“…Most interestingly, this inorganic sulphur is crucial for the activity of both FDHs and members of the xanthine oxidase family, while its functional significance in periplasmic nitrate reductases remains to be established 10,11 . In Escherichia coli, the FDH activity requires the protein FdhD that was reported to act as a sulphurtransferase between the L-cysteine desulphurase IscS and FDHs 11 . Residues Cys121 and Cys124 of EcFdhD have been shown to be involved in this reaction.…”

mentioning

confidence: 99%

“…Interestingly, the structure of an FdhD homologue in the d-proteobacteria Desulfotalea psychrophila has been solved (DpFdhD; pdb code 2PW9, unpublished) and revealed that it has structural homologies with the cytidine deaminase family of nucleotide-interacting proteins 13 . As nucleotides are chemical moieties of the Mo-bisPGD structure 14 , it has been hypothesized that EcFdhD could bind and sulphurate the cofactor before its insertion into FDHs 11 . A recent study supports this hypothesis with the copurification of Mo-bisPGD onto FdsC, an FdhD homologue from Rhodobacter capsulatus 15 .…”

mentioning

confidence: 99%

See 4 more Smart Citations

Sulphur shuttling across a chaperone during molybdenum cofactor maturation

et al. 2015

Self Cite

View full text Add to dashboard Cite

Formate dehydrogenases (FDHs) are of interest as they are natural catalysts that sequester atmospheric CO 2 , generating reduced carbon compounds with possible uses as fuel. FDHs activity in Escherichia coli strictly requires the sulphurtransferase EcFdhD, which likely transfers sulphur from IscS to the molybdenum cofactor (Mo-bisPGD) of FDHs. Here we show that EcFdhD binds Mo-bisPGD in vivo and has submicromolar affinity for GDP-used as a surrogate of the molybdenum cofactor's nucleotide moieties. The crystal structure of EcFdhD in complex with GDP shows two symmetrical binding sites located on the same face of the dimer. These binding sites are connected via a tunnel-like cavity to the opposite face of the dimer where two dynamic loops, each harbouring two functionally important cysteine residues, are present. On the basis of structure-guided mutagenesis, we propose a model for the sulphuration mechanism of Mo-bisPGD where the sulphur atom shuttles across the chaperone dimer.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Ecfdhd Is a Dimer That Binds The Molybdenum Cofactor In Vivomentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Sulphur shuttling across a chaperone during molybdenum cofactor maturation

et al. 2015

Self Cite

View full text Add to dashboard Cite

show abstract

Assembly ofMoco inMo/WEnzymes

Leimkühler

2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

The biosynthesis of the molybdenum cofactor (Moco) is ubiquitous and highly conserved in all organisms from bacteria to humans. In Moco, the molybdenum atom is coordinated to a dithiolene group present in the pterin‐based 6‐alkyl side chain of molybdopterin (MPT). In general, the biosynthesis of Moco can be divided into three steps in eukaryotes, and four steps in bacteria and archaea: (i) the starting point is the formation of the cPMP from 5′GTP, (ii) in the second step MPT is formed by the insertion of two sulfur molecules into cPMP, (iii) in the third step the molybdenum atom is inserted into MPT and Moco is formed, and (iv) additional modification of Moco occurs in bacteria and archaea in a fourth step by the attachment of nucleotides (CMP or GMP) to the phosphate group of MPT, forming the dinucleotide variants of Moco. Further, small differences exist in Moco formation among the different phyla. In higher eukaryotes Moco biosynthesis is located in different cellular compartments, many individual Moco biosynthesis proteins appear to have several cellular roles, and some proteins are shared between different biosynthetic pathways. Further, bacteria contain a large variety of more than 60 different molybdoenzymes being involved in specific, however, usually nonessential redox reactions. In contrast, in humans only four different molybdoenzymes have been identified, and a defect in Moco biosynthesis is lethal due to the loss of sulfite oxidase activity. This review will focus on the biosynthesis of Moco in bacteria and humans.

show abstract

TheW/SeCys‐FdhABformate dehydrogenase fromDesulfovibriovulgarisHildenborough

Oliveira

Mota

Romão

et al. 2022

Encyclopedia of Inorganic and Bioinorganic Chemistry

View full text Add to dashboard Cite

The W/SeCys‐FdhAB formate dehydrogenase from Desulfovibrio vulgaris Hildenborough is a dimeric periplasmic enzyme that catalyzes the reversible oxidation of formate and reduction of CO 2 . It belongs to the group of metal‐dependent FDHs, with a tungsten at the active site coordinated by two pyranopterin guanine dinucleotides, a selenocysteine, and one labile sulfur atom. FdhAB has a remarkably high activity and unusual tolerance to oxygen, making it an ideal model system to study biological CO 2 reduction.

show abstract

A Sulfurtransferase Is Essential for Activity of Formate Dehydrogenases in Escherichia coli

Cited by 75 publications

References 45 publications

Sulphur shuttling across a chaperone during molybdenum cofactor maturation

Sulphur shuttling across a chaperone during molybdenum cofactor maturation

Assembly ofMoco inMo/WEnzymes

TheW/SeCys‐FdhABformate dehydrogenase fromDesulfovibriovulgarisHildenborough

Contact Info

Product

Resources

About