PXD028742

PXD028742 is an original dataset announced via ProteomeXchange.

Title	Identification and characterization of Formate dehydrogenases (FDHs) from Bacillus subtilis
Description	The Mo/W-bisPGD Formate Dehydrogenases (FDHs) family interplays in several metabolic pathways ranging from carbon fixation to energy harvesting owing to their reaction with a wide variety of redox partners. Here, we have unveiled two non-canonical FDHs in Bacillus subtilis which are organized into two-subunit complexes, as shown by mass spectrometry, with unique features, ForCE1 and ForCE2. The ForC catalytic subunit interacts with an unprecedented partner subunit ForE and its amino acid sequence within the active site deviates from the consensus residues typically associated to FDH activity, with an histidine residue naturally substituted by a glutamine. The ForE essential subunit mediates the utilization of menaquinone as electron acceptor as shown by the formate:menadione oxidoreductase activity of both enzymes, their copurification with menaquinone and the distinctive detection of a protein-bound neutral menasemiquinone radical by multifrequency EPR experiments on the purified enzymes. Moreover, EPR characterization of both FDHs reveals the presence of several [Fe-S] clusters with distinct relaxation properties and a weakly anisotropic Mo(V) EPR signature consistent with the characteristic Mo-bisPGD cofactor of this enzyme family. Altogether, this work enlarges our representation of the FDH family by deciphering a non-canonical FDH, which differs both in terms of architecture, amino acid conservation around the Mo cofactor and reactivity.
HostingRepository	PRIDE
AnnounceDate	2022-02-16
AnnouncementXML	Submission_2022-02-16_03:37:46.396.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD028742
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Regine Lebrun
SpeciesList	scientific name: Bacillus subtilis subsp. subtilis str. 168; NCBI TaxID: 224308;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2021-09-24 11:01:22	ID requested
⏵ 1	2022-02-16 03:37:47	announced

Arias-Cart, í, n R, Uzel A, Seduk F, Gerbaud G, Pierrel F, Broc M, Lebrun R, Guigliarelli B, Magalon A, Grimaldi S, Walburger A, Identification and characterization of a noncanonical menaquinone-linked formate dehydrogenase. J Biol Chem, 298(2):101384(2022) [pubmed]

submitter keyword: Bacteria, Bacillus subtilis, purification, LC-MSMS

Regine Lebrun
contact affiliation	Aix-Marseille Univ, CNRS,FR3479, Proteomics facility of Institut de Microbiologie de la Mediterranee, Marseille Proteomique, Marseille, France
contact email	rlebrun@imm.cnrs.fr
lab head
Regine Lebrun
contact affiliation	CNRS
contact email	rlebrun@imm.cnrs.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD028742
     1. Label: PRIDE project
     2. Name: Identification and characterization of Formate dehydrogenases (FDHs) from Bacillus subtilis