PXD040248

PXD040248 is an original dataset announced via ProteomeXchange.

Title	Carbon fixation in the chemolithoautotrophic bacterium Aquifex aeolicus involves two low-potential ferredoxins as partners of the pentameric PFOR and OGOR enzymes
Description	Aquifex aeolicus is a microaerophilic hydrogen- and sulfur -oxidizing bacterium that assimilates CO2 via the reverse tricarboxylic acid cycle (rTCA). Key enzymes of this pathway are pyruvate:ferredoxin oxidoreductase (PFOR) and 2-oxoglutarate:ferredoxin oxidoreductase (OGOR), which are responsible, respectively, for the reductive carboxylation of acetyl-CoA to pyruvate and of succinyl-CoA to 2-oxoglutarate, two energetically unfavorable reactions that require a strong reduction potential. We have confirmed, by biochemistry and proteomics, that A. aeolicus possesses a pentameric version of these enzyme complexes ((αβγδε)2) and that they are highly abundant in the cell. In addition, we have purified and characterized from the soluble fraction of A. aeolicus, two low redox potential and oxygen-stable [4Fe-4S] ferredoxins (Fd6 and Fd7, E0 = -440 and -460 mV respectively) and have shown that they can physically interact and exchange electrons with both PFOR and OGOR, suggesting that they could be the physiological electron donors of the system in vivo. Shotgun proteomics indicated that all the enzymes assumed to be involved in the rTCA cycle are produced in the A. aeolicus cells. A number of additional enzymes, previously suggested to be part of a putative partial Wood-Ljungdahl pathway used for the synthesis of serine and glycine from CO2 [1], were identified by mass spectrometry, but their abundance in the cell seem to be much lower than those of the rTCA cycle. Their possible involvement in the carbon assimilation is discussed. 1- Braakman, R.; Smith, E. Metabolic Evolution of a Deep-Branching Hyperthermophilic Chemoautotrophic Bacterium. PloS One 2014, 9, e87950, doi:10.1371/journal.pone.0087950.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:47:32.638.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Regine Lebrun
SpeciesList	scientific name: Aquifex aeolicus; NCBI TaxID: 63363;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2023-02-18 01:55:37	ID requested
1	2023-05-10 14:26:07	announced
⏵ 2	2023-11-14 08:47:41	announced	2023-11-14: Updated project metadata.

Prioretti L, D'Ermo G, Infossi P, Kpebe A, Lebrun R, Bauzan M, Lojou E, Guigliarelli B, Giudici-Orticoni MT, Guiral M, Involves Two Low-Potential Ferredoxins as Partners of the PFOR and OGOR Enzymes. Life (Basel), 13(3):(2023) [pubmed]

submitter keyword: Carbon fixation

reverse TCA cycle

low potential ferredoxin

pyruvate:ferredoxin oxidoreductase

oxoglutarate:ferredoxin oxidoreductase

Wood-Ljungdahl pathway

chemolithoautotrophic bacteria

hyperthermophilic bacteria

hydrogenase

Lebrun Regine
contact affiliation	Proteomic Platform of Institut de Microbiologie de la Méditerranée CNRS FR 3479
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. PXD040248
     1. Label: PRIDE project
     2. Name: Carbon fixation in the chemolithoautotrophic bacterium Aquifex aeolicus involves two low-potential ferredoxins as partners of the pentameric PFOR and OGOR enzymes