ArticleFrontiers in chemistry2021
The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes.
Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Adaptations in electron transport chain complexes of clinical Rhodococcus equi revealed through comparative genomics.World journal of microbiology & biotechnology · 2026Article
- Linking NrfD/PsrC-like architecture to energy conservation: Functional residues in the quinone reactive QrcABCD complex of sulfate-reducing bacteria.Protein science : a publication of the Protein Society · 2026Article
- The genetic repertoire underlying electrogenic sulphur oxidation in cable bacteria.BMC genomics · 2026Article
- Demonstration of the Role of Both a Ttr and a Psr Homologue Enzymes in the Respiration of Tetrathionate by an Environmental Bacterium Shewanella sp. ANA-3.Environmental microbiology · 2026Article
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- Editorial: Computational and experimental insights in proton and ion translocating bioenergetic systems.Frontiers in chemistry · 2024Article
- Oxygen respiration and polysaccharide degradation by a sulfate-reducing acidobacterium.Nature communications · 2023Article
- Novel and unusual genes for nitrogen and metal cycling in Planctomycetota- and KSB1-affiliated metagenome-assembled genomes reconstructed from a marine subsea tunnel.FEMS microbiology letters · 2023Article
- Article
- Into the darkness: the ecologies of novel 'microbial dark matter' phyla in an Antarctic lake.Environmental microbiology · 2022Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit. The periplasmic nitrite reductase (NrfABCD) was the first complex recognized to have a membrane subunit with these characteristics and consequently provided the family's name: NrfD. Sequence analyses indicate that NrfD homologs are present in many diverse enzymes, such as polysulfide reductase (PsrABC), respiratory alternative complex III (ACIII), dimethyl sulfoxide (DMSO) reductase (DmsABC), tetrathionate reductase (TtrABC), sulfur reductase complex (SreABC), sulfite dehydrogenase (SoeABC), quinone reductase complex (QrcABCD), nine-heme cytochrome complex (NhcABCD), group-2 [NiFe] hydrogenase (Hyd-2), dissimilatory sulfite-reductase complex (DsrMKJOP), arsenate reductase (ArrC) and multiheme cytochrome
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