The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The target is PedH, encoded by pedH (ordered locus PP_2679) in Pseudomonas putida (KT2440), and described as a lanthanide-dependent pyrroloquinoline quinone (PQQ)-dependent alcohol/ethanol dehydrogenase. This exact locus tag (PP_2679) and function are consistently used in primary studies on the KT2440 PedE/PedH system, matching the UniProt accession Q88JH0 context provided by the user. (wehrmann2018thepeds2pedr2twocomponent pages 2-3, wehrmann2017functionalroleofa pages 4-7, wehrmann2017functionalroleofa pages 1-2)
PedH belongs to a family of periplasmic quinoprotein alcohol dehydrogenases that use the redox cofactor PQQ to catalyze oxidation of alcohols (and in some cases aldehydes). In P. putida KT2440, PedH and its paralog PedE constitute a periplasmic oxidation system important for detoxification and catabolism of volatile alcohols/aldehydes. (wehrmann2017functionalroleofa pages 1-2, wehrmann2019rareearthelement pages 1-2)
KT2440 encodes two functionally redundant but metal-differentiated enzymes:
- PedE (PP_2674): Ca2+-dependent PQQ-ADH
- PedH (PP_2679): Ln3+-dependent PQQ-ADH
Their expression is inversely regulated by rare earth element (REE; lanthanide) availability (“REE switch” / “lanthanide switch”), enabling the organism to deploy the metal-appropriate enzyme depending on which metals are bioavailable. (wehrmann2018thepeds2pedr2twocomponent pages 2-3, wehrmann2019rareearthelement pages 2-3)
PedH is a PQQ-dependent alcohol dehydrogenase (EC 1.1.2.- class context) functioning in the periplasmic oxidation system. It oxidizes a broad range of alcohol substrates, including linear and aromatic primary and secondary alcohols, and can show activity with some aldehydes, with substrate scope broadly similar to the Ca-dependent PedE. (wehrmann2017functionalroleofa pages 4-7, wehrmann2017functionalroleofa pages 2-4)
Experimentally supported substrates and pathway contexts in KT2440 include:
- 2-phenylethanol (growth-linked; periplasmic oxidation system) (wehrmann2019rareearthelement pages 1-2, wehrmann2018thepeds2pedr2twocomponent pages 2-3)
- glycerol (initiates an auxiliary glycerol catabolic route; see below) (wehrmann2020thecellularresponse pages 4-6)
- (2S,3S)-2,3-butanediol → acetoin (PedE/PedH responsible for the dehydrogenation step; acetoin then enters metabolism via the acetoin dehydrogenase system) (liu2021dehydrogenationmechanismof pages 1-2)
In vitro assays in the glycerol study detected PedE/PedH activity with 2-phenylethanol and glycerol but not with citrate or glucose under the tested conditions. (wehrmann2020thecellularresponse pages 4-6)
PedH is catalytically active only in the presence of trivalent lanthanides (Ln3+) and is inactive with several tested heavy lanthanides/other trivalent metals. In purified-enzyme assays, activity was observed with light-to-mid lanthanides such as La3+, Ce3+, Pr3+, Nd3+, Sm3+, Gd3+, Tb3+, while Er3+, Yb3+, Y3+, Sc3+ did not support activity under the reported assay conditions; the highest activities were reported with Pr3+ and Nd3+. (wehrmann2017functionalroleofa pages 4-7, wehrmann2017functionalroleofa pages 2-4)
These metal preferences are visualized in the lanthanide-dependence figure for PedH activity across rare earth metal ions. (wehrmann2017functionalroleof media a288382e)
A key mechanistic distinction between PedH and PedE is PedH’s much higher affinity for lanthanides than PedE’s affinity for Ca2+.
From purified-enzyme measurements (selected examples):
- Lanthanide binding affinity (PedH): KD ~25–75 nM; enzyme active over ~10 nM to 100 µM Ln, with peak around ~1 µM (wehrmann2017functionalroleofa pages 4-7, wehrmann2017functionalroleof pages 6-10)
- Ethanol kinetics (PedH vs PedE): Vmax(PedH) ≈ 10.6 U·mg−1 vs Vmax(PedE) ≈ 6.1 U·mg−1; KM(PedH) ~177 µM vs KM(PedE) ~85 µM (wehrmann2017functionalroleofa pages 4-7)
The kinetic parameter panel/table for PedH is shown in the retrieved figure crop. (wehrmann2017functionalroleof media 5ce5386c)
PedH contains a conserved active-site Asp (contrasting with a Ser in PedE) that is associated with Ln3+ coordination in lanthanide-dependent quinoprotein dehydrogenases. (wehrmann2017functionalroleofa pages 2-4)
PedH is explicitly described as part of a periplasmic oxidation system (together with PedE) that supports growth on alcoholic substrates and influences substrate-dependent physiology (e.g., glycerol growth behavior). (wehrmann2019rareearthelement pages 1-2, wehrmann2020thecellularresponse pages 4-6)
Growth on volatile alcohols (e.g., 2-phenylethanol):
PedH is required for efficient growth in conditions where lanthanides drive the system toward PedH usage. For example, in the presence of lanthanides (La3+), a ΔpedH strain fails to grow on 2-phenylethanol under conditions where the REE switch represses reliance on PedE, demonstrating the ecological role of PedH as the Ln-dependent branch of the periplasmic oxidation system. (wehrmann2018thepeds2pedr2twocomponent pages 2-3, wehrmann2018thepeds2pedr2twocomponent pages 3-5)
Glycerol metabolism (auxiliary route):
A substrate-specific lanthanum response study linked PedE/PedH activity to a novel glycerol route: oxidation of glycerol to glyceraldehyde and then to glycerate, followed by phosphorylation by GarK, providing an advantage in lag-phase behavior. PedE/PedH form the “periplasmic oxidation system” implicated in initiating this alternative route. (wehrmann2020thecellularresponse pages 4-6, wehrmann2020thecellularresponse pages 2-4)
2,3-butanediol catabolism:
PedH and PedE were confirmed as the enzymes responsible for dehydrogenation of (2S,3S)-2,3-butanediol to acetoin, feeding acetoin into central metabolism via the acetoin dehydrogenase complex. (liu2021dehydrogenationmechanismof pages 1-2)
A central mechanistic advance for KT2440 is that the REE switch is orchestrated by the PedS2/PedR2 two-component system (TCS):
- No lanthanides: PedS2 phosphorylates PedR2; phosphorylated PedR2 activates pedE transcription and represses pedH.
- Lanthanides present: PedS2 kinase activity is reduced (possibly by Ln binding to the periplasmic region), decreasing PedR2 phosphorylation; this relieves pedH repression and shifts the cell toward PedH-dependent oxidation (with additional positive feedback proposed for PedH). (wehrmann2018thepeds2pedr2twocomponent pages 2-3, wehrmann2018thepeds2pedr2twocomponent pages 8-9)
Adaptive evolution of a ΔpedH strain under La3+ selection produced suppressors with pedS2 mutations (e.g., S178P in a HAMP domain), which restored growth and decoupled pedE promoter activity from La3+ availability. For the PedS2 S178P allele, pedE promoter activities were reported as nearly identical ±La3+ (ratio ~0.89 ± 0.02) and increased >24-fold relative to the parental ΔpedH in the absence of La3+. (wehrmann2018thepeds2pedr2twocomponent pages 3-5)
Efficient growth on 2-phenylethanol at low (nanomolar) lanthanide concentrations depends on an ABC-type transporter encoded by pedA1A2BC; without it, ~100-fold higher La3+ is needed for PedH-dependent growth (while repression of PedE can still occur). Iron (and other metals) can strongly influence the effective Ln threshold for switching, consistent with mismetallation/competition affecting sensing proteins such as PedS2. (wehrmann2019rareearthelement pages 2-3)
A major 2024 update is that the PedE/PedH lanthanide switch behaves as element-dependent transcript-pool tuning rather than a simple binary “PedE off / PedH on” response.
In Pseudomonas alloputida KT2440 (same KT2440 strain lineage used widely in the PedH literature), Gorniak et al. (published Oct 2024) showed:
- Growth effects at low La: maximal growth rate 1.64 ± 0.13 h−1 and minimum doubling time 0.42 ± 0.03 h at 10–50 nM La, compared to 0.88 ± 0.06 h−1 without added Ln (gorniak2024changesingrowth pages 2-5)
- Element-specific transcriptional tuning: pedE transcript abundance varied dramatically by Ln; for example pedE RPKM was 410.28 ± 56.55 (no Ln), 210.45 ± 27.53 (Er), and 3.25–4.45 (light Ln La–Nd), and pedH expression increased ~1.9–4.2× (Nd–La) (gorniak2024changesingrowth pages 9-11)
- Light vs heavy Ln: heavy Ln (e.g., Er) behave differently from light Ln in gene expression and growth; because PedH is inactive with heavy Ln such as Er/Yb, heavy Ln can impose fitness costs potentially via mismetallation and interference with Ln sensing/signaling (gorniak2024changesingrowth pages 9-11)
The same 2024 work quantified cell-associated lanthanides after exposure to 1 µM Ln using single-cell ICP-MS, reporting (examples): 0.058 ± 0.055 fg La/cell, 0.125 ± 0.086 fg Nd/cell, 0.152 ± 0.106 fg Er/cell, corresponding to ~0.0025%–0.0068% of wet weight. (gorniak2024changesingrowth pages 2-5, gorniak2024changesingrowth pages 11-13)
PedH-like lanthanide-dependent PQQ-ADHs have been explicitly proposed as enabling technologies: biocatalysts, biosensors, and microbial platforms for biomining/bioleaching/recycling of rare earth metals. (wehrmann2017functionalroleofa pages 2-4, wehrmann2017functionalroleof pages 1-6)
In KT2440 specifically, PedH (and the REE switch) provides a tunable periplasmic oxidation capability supporting growth on volatile alcohols and modulating glycerol physiology; these attributes are relevant for industrial biotechnology contexts where P. putida is used as a robust chassis and where media metal composition can affect performance. (wehrmann2020thecellularresponse pages 4-6, wehrmann2019rareearthelement pages 2-3)
A recent global-ocean metagenomic analysis (preprint 2023; journal publication Jul 2025) found 6,886 PQQ dehydrogenases in ocean metagenomes, with 56% containing a lanthanide-binding motif, and lanthanide-dependent genes in ~20% of resolved microbial genomes; the authors note some organisms may be targets for lanthanophore-based biomining and purification. While not specific to PedH in KT2440, these statistics strengthen the case that lanthanide-dependent PQQ-DHs are widespread “real-world” biological implementations and potential resources for biotechnology. (voutsinos2025extensiveanddiverse pages 1-3)
Functional core: PedH is best understood as a periplasmic, lanthanide-activated PQQ alcohol dehydrogenase that broadens KT2440’s ability to oxidize diverse alcohols under environmentally realistic Ln conditions, with higher catalytic capacity and much tighter metal binding than the Ca-dependent paralog PedE. (wehrmann2017functionalroleofa pages 4-7, wehrmann2019rareearthelement pages 1-2)
Metal-driven niche adaptation: The PedE/PedH system is not simply redundant; it is regulated by a dedicated sensory TCS (PedS2/PedR2) and appears tuned for fluctuating metal microenvironments (e.g., rhizosphere/soil), enabling rapid switching to the metal that yields higher fitness on available substrates. (wehrmann2018thepeds2pedr2twocomponent pages 2-3, wehrmann2019rareearthelement pages 2-3)
2024 refinement: The latest KT2440 work shows the “lanthanide switch” is element-discriminating and quantitatively tuned at transcript and growth levels; this is consistent with a model where sensing/signaling and enzyme metallation can be perturbed by non-utilizable heavy lanthanides, potentially causing mismetallation and suboptimal expression of PedE. (gorniak2024changesingrowth pages 9-11, gorniak2024changesingrowth pages 2-5)
The following table compiles the main functional and regulatory claims, quantitative parameters, and 2024 updates with URLs/DOIs.
| Category | Specific findings (with numbers) | Evidence/source (first author year journal) | URL/DOI |
|---|---|---|---|
| Identity | pedH = PP_2679 = UniProt Q88JH0 in Pseudomonas putida KT2440; characterized as a lanthanide-dependent PQQ alcohol/ethanol dehydrogenase that is inversely regulated with PedE (PP_2674). (wehrmann2018thepeds2pedr2twocomponent pages 2-3, wehrmann2017functionalroleofa pages 1-2) | Wehrmann 2017 mBio; Wehrmann 2018 mSphere | https://doi.org/10.1128/mbio.00570-17; https://doi.org/10.1128/msphere.00376-18 |
| Core biochemical function | Periplasmic PQQ-dependent alcohol dehydrogenase in a periplasmic oxidation system; catalyzes oxidation of alcohols/aldehydes important for growth on alcoholic volatiles, including 2-phenylethanol. (wehrmann2019rareearthelement pages 1-2, wehrmann2017functionalroleofa pages 1-2) | Wehrmann 2019 Front. Microbiol.; Wehrmann 2017 mBio | https://doi.org/10.3389/fmicb.2019.02494; https://doi.org/10.1128/mbio.00570-17 |
| Metal cofactor requirement | PedH is active only with Ln³⁺; active with La³⁺, Ce³⁺, Pr³⁺, Nd³⁺, Sm³⁺, Gd³⁺, Tb³⁺; inactive with Er³⁺, Yb³⁺, Y³⁺, Sc³⁺ under tested conditions. Peak activity reported with Pr³⁺/Nd³⁺. (wehrmann2017functionalroleofa pages 4-7, wehrmann2017functionalroleofa pages 2-4) | Wehrmann 2017 mBio | https://doi.org/10.1128/mbio.00570-17 |
| Substrate scope | Broad substrate range similar to PedE: linear and aromatic primary/secondary alcohols and some aldehydes; example substrates include ethanol, 1-butanol, 2-phenylethanol, glycerol, 2,3-butanediol. Methanol is a poor substrate. (wehrmann2017functionalroleofa pages 2-4, wehrmann2020thecellularresponse pages 4-6, liu2021dehydrogenationmechanismof pages 1-2) | Wehrmann 2017 mBio; Wehrmann 2020 mBio; Liu 2021 Front. Bioeng. Biotechnol. | https://doi.org/10.1128/mbio.00570-17; https://doi.org/10.1128/mbio.00516-20; https://doi.org/10.3389/fbioe.2021.728767 |
| Kinetics and affinity | Under optimized assays, Vmax ≈ 10.6 U mg⁻¹ for ethanol vs 6.1 U mg⁻¹ for PedE; Km(ethanol) ≈ 177 µM vs PedE ≈ 85 µM; Ln binding Kd ≈ 25–75 nM, far tighter than PedE Ca²⁺ binding (~64 µM). PedH active from 10 nM to 100 µM Ln, peak around 1 µM. (wehrmann2017functionalroleofa pages 4-7, wehrmann2017functionalroleof pages 6-10, wehrmann2017functionalroleof media 5ce5386c) | Wehrmann 2017 mBio | https://doi.org/10.1128/mbio.00570-17 |
| Representative specific activities | Example activities higher than PedE for several substrates: ethanol ~11.0 vs 6.7 U mg⁻¹, 1-butanol ~11.5 vs 5.8 U mg⁻¹ (PedH vs PedE). On glycerol, PedH 0.9 ± 0.1 U mg⁻¹ vs PedE 0.3 ± 0.1 U mg⁻¹. (wehrmann2017functionalroleofa pages 2-4, wehrmann2020thecellularresponse pages 4-6) | Wehrmann 2017 mBio; Wehrmann 2020 mBio | https://doi.org/10.1128/mbio.00570-17; https://doi.org/10.1128/mbio.00516-20 |
| Localization / cell compartment | Explicitly described as part of a periplasmic oxidation system; PedE/PedH periplasmic oxidation contributes to detoxification/catabolism of volatile alcohols and glycerol-related metabolism. (wehrmann2020thecellularresponse pages 4-6, wehrmann2019rareearthelement pages 1-2, wehrmann2017functionalroleofa pages 1-2) | Wehrmann 2020 mBio; Wehrmann 2019 Front. Microbiol.; Wehrmann 2017 mBio | https://doi.org/10.1128/mbio.00516-20; https://doi.org/10.3389/fmicb.2019.02494; https://doi.org/10.1128/mbio.00570-17 |
| Pathway context: volatile alcohols | Expression of either PedE or PedH is required for efficient growth on volatile alcohols; ΔpedH shows impaired/no growth on 2-phenylethanol when La³⁺ is present, consistent with the Ln switch forcing dependence on PedH. (wehrmann2018thepeds2pedr2twocomponent pages 2-3, wehrmann2017functionalroleofa pages 4-7) | Wehrmann 2018 mSphere; Wehrmann 2017 mBio | https://doi.org/10.1128/msphere.00376-18; https://doi.org/10.1128/mbio.00570-17 |
| Pathway context: glycerol | PedE/PedH initiate a novel glycerol route parallel to glpFKRD: glycerol oxidation proceeds via glyceraldehyde → glycerate, then GarK phosphorylates glycerate for entry into central metabolism. Presence of PedH shortens lag on glycerol. (wehrmann2020thecellularresponse pages 2-4, wehrmann2020thecellularresponse pages 4-6) | Wehrmann 2020 mBio | https://doi.org/10.1128/mbio.00516-20 |
| Pathway context: 2,3-butanediol | PedE/PedH are responsible for (2S,3S)-2,3-butanediol dehydrogenation to acetoin; acetoin then enters metabolism via the acetoin dehydrogenase enzyme system. (liu2021dehydrogenationmechanismof pages 1-2) | Liu 2021 Front. Bioeng. Biotechnol. | https://doi.org/10.3389/fbioe.2021.728767 |
| REE switch regulation | PedS2/PedR2 is the key two-component system for the rare-earth-element switch. In no Ln, PedS2 phosphorylates PedR2, which activates pedE and represses pedH; with Ln, PedS2 kinase activity drops, relieving pedH repression and shifting cells toward PedH-dependent oxidation. (wehrmann2018thepeds2pedr2twocomponent pages 2-3) | Wehrmann 2018 mSphere | https://doi.org/10.1128/msphere.00376-18 |
| Quantitative regulation / mutants | In a ΔpedH background, suppressor mutations in pedS2 restore growth with La³⁺; the PedS2 S178P allele gave nearly identical pedE promoter activity with vs without La³⁺ (ratio ~0.89 ± 0.02) and >24-fold higher activity than the ΔpedH parent; ΔpedH otherwise showed no growth within 72 h under tested La³⁺ conditions. (wehrmann2018thepeds2pedr2twocomponent pages 3-5) | Wehrmann 2018 mSphere | https://doi.org/10.1128/msphere.00376-18 |
| Lanthanide uptake / metal homeostasis | Efficient PedH-dependent growth at low Ln requires PedA1A2BC ABC transporter; without it, about ~100-fold higher La³⁺ is needed for PedH-dependent growth on 2-phenylethanol. Iron, copper, and zinc alter the REE switch, likely via mismetallation/competition. (wehrmann2019rareearthelement pages 2-3, gorniak2024changesingrowth pages 11-13) | Wehrmann 2019 Front. Microbiol.; Gorniak 2024 mSphere | https://doi.org/10.3389/fmicb.2019.02494; https://doi.org/10.1128/msphere.00685-24 |
| 2024 update: growth effects of light vs heavy Ln | In KT2440, the Ln switch is element-specific. La/Ce/Nd and an Ln mix improved growth; heavy Ln impaired growth. Best performance occurred at 10–50 nM La, with growth rate 1.64 ± 0.13 h⁻¹ and doubling time 0.42 ± 0.03 h, versus 0.88 ± 0.06 h⁻¹ without Ln. Er caused little benefit and could impair fitness. (gorniak2024changesingrowth pages 2-5) | Gorniak 2024 mSphere | https://doi.org/10.1128/msphere.00685-24 |
| 2024 update: pedE/pedH transcript tuning | 2024 RNA-seq showed the switch is a fine-tuning of pedE/pedH transcript pools, not a binary on/off. pedE RPKM: 410.28 ± 56.55 (no Ln), 210.45 ± 27.53 (Er), 3.25–4.45 (La–Nd). pedE:pedH ratio: ~6 (no Ln), ~2 (Er), shifted toward pedH with La/Nd/mix; pedH increased 1.9–4.2×, and RT-qPCR showed 2.4-fold pedH increase with La. (gorniak2024changesingrowth pages 9-11) | Gorniak 2024 mSphere | https://doi.org/10.1128/msphere.00685-24 |
| 2024 update: cell-associated lanthanides | Single-cell ICP-MS after 1 µM exposure measured 0.058 ± 0.055 fg La/cell, 0.125 ± 0.086 fg Nd/cell, 0.152 ± 0.106 fg Er/cell, corresponding to about 0.0025%–0.0068% wet weight. Heavy-Ln effects were interpreted as possible mismetallation and altered sensing/signaling. (gorniak2024changesingrowth pages 2-5, gorniak2024changesingrowth pages 11-13) | Gorniak 2024 mSphere | https://doi.org/10.1128/msphere.00685-24 |
| Structural/sequence inference | PedH contains an active-site Asp (vs Ser in Ca²⁺-dependent PedE), a hallmark associated with Ln³⁺ coordination in XoxF/ExaF/PedH-type quinoprotein dehydrogenases. (wehrmann2017functionalroleofa pages 2-4) | Wehrmann 2017 mBio | https://doi.org/10.1128/mbio.00570-17 |
| Application relevance | PedH-like Ln-dependent PQQ-ADHs are discussed as candidates for biocatalysts, biosensors, and for microbial biomining/bioleaching/recycling of rare earth elements. Broader studies indicate Ln-dependent PQQ-DHs are widespread: 6,886 PQQ-DH proteins detected in ocean metagenomes, 56% with the Ln-binding motif, and Ln-dependent genes in ~20% of resolved genomes. (wehrmann2017functionalroleof pages 1-6, voutsinos2025extensiveanddiverse pages 1-3, skovran2019lanthanidesinmethylotrophy pages 1-2) | Wehrmann 2017 mBio; Voutsinos 2025 ISME J.; Skovran 2019 Curr. Issues Mol. Biol. | https://doi.org/10.1128/mbio.00570-17; https://doi.org/10.1101/2023.07.25.550467; https://doi.org/10.21775/cimb.033.101 |
Table: This table condenses the key functional, biochemical, regulatory, and recent 2024 findings for PedH (PP_2679/Q88JH0) in Pseudomonas putida KT2440. It is designed as a data-rich reference linking each major claim to specific primary sources and URLs/DOIs.
The provided evidence set supports periplasmic localization and broad biochemical activity, but does not fully resolve the in vivo physiological electron acceptor chain (e.g., specific cytochromes or membrane electron carriers) for PedH in KT2440; the studies commonly use DCPIP-based assays for activity quantification and focus on growth/regulation outcomes rather than the complete periplasmic electron transfer network. (wehrmann2020thecellularresponse pages 4-6)
References
(wehrmann2018thepeds2pedr2twocomponent pages 2-3): Matthias Wehrmann, Charlotte Berthelot, Patrick Billard, and Janosch Klebensberger. The peds2/pedr2 two-component system is crucial for the rare earth element switch in pseudomonas putida kt2440. mSphere, Aug 2018. URL: https://doi.org/10.1128/msphere.00376-18, doi:10.1128/msphere.00376-18. This article has 41 citations and is from a peer-reviewed journal.
(wehrmann2017functionalroleofa pages 4-7): Matthias Wehrmann, Patrick Billard, Audrey Martin-Meriadec, Asfaw Zegeye, and Janosch Klebensberger. Functional role of lanthanides in enzymatic activity and transcriptional regulation of pyrroloquinoline quinone-dependent alcohol dehydrogenases in pseudomonas putida kt2440. mBio, Jul 2017. URL: https://doi.org/10.1128/mbio.00570-17, doi:10.1128/mbio.00570-17. This article has 218 citations and is from a domain leading peer-reviewed journal.
(wehrmann2017functionalroleofa pages 1-2): Matthias Wehrmann, Patrick Billard, Audrey Martin-Meriadec, Asfaw Zegeye, and Janosch Klebensberger. Functional role of lanthanides in enzymatic activity and transcriptional regulation of pyrroloquinoline quinone-dependent alcohol dehydrogenases in pseudomonas putida kt2440. mBio, Jul 2017. URL: https://doi.org/10.1128/mbio.00570-17, doi:10.1128/mbio.00570-17. This article has 218 citations and is from a domain leading peer-reviewed journal.
(wehrmann2019rareearthelement pages 1-2): Matthias Wehrmann, Charlotte Berthelot, Patrick Billard, and Janosch Klebensberger. Rare earth element (ree)-dependent growth of pseudomonas putida kt2440 relies on the abc-transporter peda1a2bc and is influenced by iron availability. Frontiers in Microbiology, Oct 2019. URL: https://doi.org/10.3389/fmicb.2019.02494, doi:10.3389/fmicb.2019.02494. This article has 40 citations and is from a peer-reviewed journal.
(wehrmann2019rareearthelement pages 2-3): Matthias Wehrmann, Charlotte Berthelot, Patrick Billard, and Janosch Klebensberger. Rare earth element (ree)-dependent growth of pseudomonas putida kt2440 relies on the abc-transporter peda1a2bc and is influenced by iron availability. Frontiers in Microbiology, Oct 2019. URL: https://doi.org/10.3389/fmicb.2019.02494, doi:10.3389/fmicb.2019.02494. This article has 40 citations and is from a peer-reviewed journal.
(wehrmann2017functionalroleofa pages 2-4): Matthias Wehrmann, Patrick Billard, Audrey Martin-Meriadec, Asfaw Zegeye, and Janosch Klebensberger. Functional role of lanthanides in enzymatic activity and transcriptional regulation of pyrroloquinoline quinone-dependent alcohol dehydrogenases in pseudomonas putida kt2440. mBio, Jul 2017. URL: https://doi.org/10.1128/mbio.00570-17, doi:10.1128/mbio.00570-17. This article has 218 citations and is from a domain leading peer-reviewed journal.
(wehrmann2020thecellularresponse pages 4-6): Matthias Wehrmann, Maxime Toussaint, Jens Pfannstiel, Patrick Billard, and Janosch Klebensberger. The cellular response to lanthanum is substrate specific and reveals a novel route for glycerol metabolism in pseudomonas putida kt2440. mBio, Apr 2020. URL: https://doi.org/10.1128/mbio.00516-20, doi:10.1128/mbio.00516-20. This article has 29 citations and is from a domain leading peer-reviewed journal.
(liu2021dehydrogenationmechanismof pages 1-2): Yidong Liu, Xiuqing Wang, Liting Ma, Min Lü, Wen Zhang, Chuanjuan Lü, Chao Gao, Ping Xu, and Cuiqing Ma. Dehydrogenation mechanism of three stereoisomers of butane-2,3-diol in pseudomonas putida kt2440. Frontiers in Bioengineering and Biotechnology, Aug 2021. URL: https://doi.org/10.3389/fbioe.2021.728767, doi:10.3389/fbioe.2021.728767. This article has 6 citations.
(wehrmann2017functionalroleof media a288382e): Matthias Wehrmann, Patrick Billard, Audrey Martin-Meriadec, Asfaw Zegeye, and Janosch Klebensberger. Functional role of lanthanides in enzymatic activity and transcriptional regulation of pyrroloquinoline quinone-dependent alcohol dehydrogenases in pseudomonas putida kt2440. mBio, Jul 2017. URL: https://doi.org/10.1128/mbio.00570-17, doi:10.1128/mbio.00570-17. This article has 218 citations and is from a domain leading peer-reviewed journal.
(wehrmann2017functionalroleof pages 6-10): Matthias Wehrmann, Patrick Billard, Audrey Martin Meriadec, Asfaw Zegeye, and Janosch Klebensberger. Functional role of lanthanides in enzymatic activity and transcriptional regulation of pqq-dependent alcohol dehydrogenases in pseudomonas putida kt2440. bioRxiv, May 2017. URL: https://doi.org/10.1101/140046, doi:10.1101/140046. This article has 1 citations.
(wehrmann2017functionalroleof media 5ce5386c): Matthias Wehrmann, Patrick Billard, Audrey Martin-Meriadec, Asfaw Zegeye, and Janosch Klebensberger. Functional role of lanthanides in enzymatic activity and transcriptional regulation of pyrroloquinoline quinone-dependent alcohol dehydrogenases in pseudomonas putida kt2440. mBio, Jul 2017. URL: https://doi.org/10.1128/mbio.00570-17, doi:10.1128/mbio.00570-17. This article has 218 citations and is from a domain leading peer-reviewed journal.
(wehrmann2018thepeds2pedr2twocomponent pages 3-5): Matthias Wehrmann, Charlotte Berthelot, Patrick Billard, and Janosch Klebensberger. The peds2/pedr2 two-component system is crucial for the rare earth element switch in pseudomonas putida kt2440. mSphere, Aug 2018. URL: https://doi.org/10.1128/msphere.00376-18, doi:10.1128/msphere.00376-18. This article has 41 citations and is from a peer-reviewed journal.
(wehrmann2020thecellularresponse pages 2-4): Matthias Wehrmann, Maxime Toussaint, Jens Pfannstiel, Patrick Billard, and Janosch Klebensberger. The cellular response to lanthanum is substrate specific and reveals a novel route for glycerol metabolism in pseudomonas putida kt2440. mBio, Apr 2020. URL: https://doi.org/10.1128/mbio.00516-20, doi:10.1128/mbio.00516-20. This article has 29 citations and is from a domain leading peer-reviewed journal.
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(gorniak2024changesingrowth pages 9-11): Linda Gorniak, Sarah Luise Bucka, Bayan Nasr, Jialan Cao, Steffen Hellmann, Thorsten Schäfer, Martin Westermann, Julia Bechwar, and Carl-Eric Wegner. Changes in growth, lanthanide binding, and gene expression in pseudomonas alloputida kt2440 in response to light and heavy lanthanides. Oct 2024. URL: https://doi.org/10.1128/msphere.00685-24, doi:10.1128/msphere.00685-24. This article has 5 citations and is from a peer-reviewed journal.
(gorniak2024changesingrowth pages 11-13): Linda Gorniak, Sarah Luise Bucka, Bayan Nasr, Jialan Cao, Steffen Hellmann, Thorsten Schäfer, Martin Westermann, Julia Bechwar, and Carl-Eric Wegner. Changes in growth, lanthanide binding, and gene expression in pseudomonas alloputida kt2440 in response to light and heavy lanthanides. Oct 2024. URL: https://doi.org/10.1128/msphere.00685-24, doi:10.1128/msphere.00685-24. This article has 5 citations and is from a peer-reviewed journal.
(wehrmann2017functionalroleof pages 1-6): Matthias Wehrmann, Patrick Billard, Audrey Martin Meriadec, Asfaw Zegeye, and Janosch Klebensberger. Functional role of lanthanides in enzymatic activity and transcriptional regulation of pqq-dependent alcohol dehydrogenases in pseudomonas putida kt2440. bioRxiv, May 2017. URL: https://doi.org/10.1101/140046, doi:10.1101/140046. This article has 1 citations.
(voutsinos2025extensiveanddiverse pages 1-3): Marcos Y. Voutsinos, Jillian F. Banfield, and Harry-Luke O. McClelland. Extensive and diverse lanthanide-dependent metabolism in the ocean. The ISME Journal, Jul 2025. URL: https://doi.org/10.1101/2023.07.25.550467, doi:10.1101/2023.07.25.550467. This article has 10 citations.
(skovran2019lanthanidesinmethylotrophy pages 1-2): Elizabeth Skovran, Charumathi Raghuraman, and Norma Cecilia Martinez-Gomez. Lanthanides in methylotrophy. Current issues in molecular biology, 33:101-116, Jan 2019. URL: https://doi.org/10.21775/cimb.033.101, doi:10.21775/cimb.033.101. This article has 49 citations.