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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 protein is the calcium-dependent pyrroloquinoline quinone (PQQ) methanol dehydrogenase large subunit of Methylorubrum extorquens strain AM1 (formerly Methylobacterium extorquens AM1), encoded by mxaF (synonym moxF) and mapped to MexAM1_META1p4538 in AM1 genome annotations. This mapping (mxaF = MexAM1_META1p4538) matches the UniProt-provided ordered locus name and the description “methanol dehydrogenase [cytochrome c] subunit 1 / large subunit alpha.” (roszczenkojasinska2020geneproductsand pages 4-5)
The literature also uses MxaF to refer to the canonical, Ca2+-dependent methanol dehydrogenase system (MxaFI) in AM1 and related methylotrophs, which is distinct from the lanthanide-dependent alternative MDH systems encoded by xoxF genes. (good2016pyrroloquinolinequinoneethanol pages 3-5, chu2016xoxfactsas pages 1-5)
MxaF is the catalytic large subunit of the classical methanol dehydrogenase MxaFI. In methylotrophic Alphaproteobacteria, MxaFI is a PQQ-linked, soluble periplasmic enzyme that oxidizes methanol during aerobic methylotrophy. (good2016pyrroloquinolinequinoneethanol pages 3-5, chu2016xoxfactsas pages 1-5)
Subunit composition: MxaFI-type MDH is typically an α2β2 heterotetramer (two MxaF + two MxaI). (good2016pyrroloquinolinequinoneethanol pages 3-5)
Cofactors: MxaFI contains PQQ as a prosthetic group and a Ca2+ ion in the active site (contrasting with XoxF enzymes that incorporate lanthanides rather than Ca2+). (good2016pyrroloquinolinequinoneethanol pages 3-5, deng2018structureandfunction pages 7-10)
Primary reaction: MxaFI catalyzes methanol oxidation to formaldehyde in the periplasm. (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5)
Electron acceptor coupling: The canonical mxa operon includes mxaG, encoding a cytochrome cL electron acceptor that couples to periplasmic PQQ alcohol dehydrogenases (including MxaFI). (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 1-4)
Many methylotrophs (including M. extorquens AM1) encode both:
- MxaFI: Ca2+/PQQ-dependent MDH (mxaF/mxaI), and
- XoxF-type: lanthanide (Ln3+)-dependent PQQ MDH.
Lanthanides can act as environmental signals that repress expression of the mxa operon and induce expression of xox genes, shifting methanol oxidation capacity toward XoxF-type enzymes (“lanthanide switch”). (roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 7-10)
In AM1, methanol oxidation is carried out in the periplasm by PQQ-dependent alcohol dehydrogenases. When lanthanides are absent, MxaFI is the sole methanol oxidizer supporting methylotrophic growth. (roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 1-4)
When lanthanides are present, XoxF enzymes oxidize methanol to formaldehyde and other Ln-dependent enzymes (e.g., ExaF) can further influence oxidation chemistry; however, MxaF itself remains the canonical Ca-dependent MDH benchmark and becomes less central as Xox systems dominate. (roszczenkojasinska2020geneproductsand pages 4-5, good2018investigationoflanthanidedependent pages 8-12)
The retrieved AM1-focused sources explicitly support methanol → formaldehyde as the core physiological reaction of MxaFI-type MDH. (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5)
They do not provide direct AM1-specific kinetic constants (Km, kcat) for MxaF/MxaFI itself; therefore, detailed substrate range beyond methanol cannot be quantified here without additional primary biochemical characterization papers. What is supported is that MxaFI belongs to the methanol/ethanol family of PQQ dehydrogenases and is assayed under alkaline conditions in vitro in related work, but this is not AM1-specific kinetic evidence for MxaF. (good2016pyrroloquinolinequinoneethanol pages 5-7)
A 2024 review summarizes the structural logic of MxaF-type MDHs: PQQ sits in the β-propeller central cavity, and the PQQ–metal complex performs oxidation of methanol to formaldehyde; the bound metal (Ca2+ in MxaF) acts as a Lewis acid to stabilize developing charges. (rocha2024rareearthelements pages 2-5)
The same review highlights a diagnostic difference vs lanthanide-dependent XoxF: the D-x-x-D-[YFW]-D motif (final Asp) that helps coordinate lanthanides in XoxF distinguishes XoxF from MxaF. (rocha2024rareearthelements pages 2-5)
Methanol oxidation in AM1 is stated to be carried out in the periplasm by PQQ-dependent alcohol dehydrogenases, including Ca2+-dependent MxaFI and Ln-dependent XoxF1. (roszczenkojasinska2020geneproductsand pages 1-4)
The AM1 mxa operon is reported as mxaFJGIRSACKLDEHB, and includes key partner proteins:
- MxaI (small subunit),
- MxaG (cytochrome cL electron acceptor),
- MxaJ (periplasmic binding/chaperone-like factor),
- and proteins implicated in Ca2+ insertion/maturation (e.g., mxaACKL). (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5)
MxaF (in MxaFI) initiates aerobic methylotrophy by producing formaldehyde from methanol in the periplasm. Formaldehyde is hazardous and must be further processed by downstream pathways; consistent with this, lanthanide-dependent methylotrophic growth still requires intracellular formaldehyde-processing capacity (e.g., dependence on fae, the formaldehyde-activating enzyme, in AM1 under lanthanide conditions). (good2018investigationoflanthanidedependent pages 8-12)
In AM1, transcription of the mxa operon is controlled by two-component systems and regulators including MxcQE, MxbDM, and MxaB. (chu2016xoxfactsas pages 1-5)
Quantitative promoter evidence in AM1: In promoter reporter assays, adding 2 μM La3+ caused the mxa promoter signal to drop from ~323 ± 63 to ~61 ± 10 RFU/OD600, while xox1 promoter activity increased from ~44 ± 3 to ~206 ± 11, consistent with the lanthanide switch. (roszczenkojasinska2020geneproductsand pages 7-10)
A key AM1 study reports that in methanol + La3+:
- Wild type grows at ~0.16 ± 0.01 h−1,
- ΔmxaF grows at ~0.16 ± 0.01 h−1 (i.e., essentially unchanged under La3+),
- ΔxoxF1 grows more slowly (~0.07 ± 0.00 h−1, with a 6–9 h lag),
- ΔxoxF1 ΔxoxF2 and ΔmxaF ΔxoxF1 ΔxoxF2 are slower still (~0.04 h−1). (roszczenkojasinska2020geneproductsand pages 6-7)
These phenotypes support the interpretation that, when lanthanides are available, AM1’s methanol growth depends strongly on the XoxF system, while MxaF becomes dispensable under these conditions. (roszczenkojasinska2020geneproductsand pages 6-7)
(Visual evidence: the growth-rate table is shown in the extracted image.) (roszczenkojasinska2020geneproductsand media fa5edca9)
A focused AM1 study of lanthanide-dependent methylotrophy reports that adding lanthanides yields 15–22% increases in growth rate and 10–12.5% increases in growth yield in methanol growth, indicating that Ln-dependent methylotrophy can be more efficient overall than Ca-dependent methylotrophy (system-level effect attributable to Ln-dependent enzymes such as XoxF1/ExaF). (good2018investigationoflanthanidedependent pages 1-5)
The same work provides example growth rates: at 15 mM methanol, specific growth rates of 0.181 ± 0.002 h−1 (+La) vs 0.157 ± 0.003 h−1 (−La). (good2018investigationoflanthanidedependent pages 8-12)
A 2024 peer-reviewed review (Microbial Biotechnology) explicitly frames MxaF as the well-characterized Ca2+ and PQQ-dependent MDH and contrasts it with XoxF enzymes that incorporate REEs instead of Ca2+. (Rocha et al., published June 2024, https://doi.org/10.1111/1751-7915.14503). (rocha2024rareearthelements pages 1-2)
This review also summarizes contemporary mechanistic understanding: PQQ–metal (Ca2+) chemistry in the β-propeller active site supports methanol oxidation to formaldehyde, and motif differences (DxxD-[YFW]-D) differentiate REE-dependent XoxF from Ca-dependent MxaF. (rocha2024rareearthelements pages 2-5)
AM1 is treated as a model for understanding how metals and periplasmic enzymes integrate with cell biology. In AM1, lanthanides drive operon-level regulation (downregulating mxa, upregulating xox1), and the system includes dedicated lanthanide transport/homeostasis genes such as the lut cluster, including lanmodulin (LanM). (roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 7-10)
Although MxaF itself is primarily studied as a methylotrophy enzyme, 2024 work connects the broader PQQ-MDH/REE biology (MxaF vs XoxF/ExaF) to practical technologies:
Rocha et al. (2024) report that M. extorquens has been used to accumulate neodymium from magnet waste and to reclaim gadolinium from medical waste, and that hyperaccumulating mutants have been reported. (rocha2024rareearthelements pages 5-6)
The 2024 review emphasizes protein-based binders and separations, notably lanmodulin (LanM): it binds lanthanides with low-picomolar KD and ~10^8-fold selectivity over Ca2+, and it has been immobilized on supports (e.g., agarose, magnetic nanoparticles, elastin-like polypeptides) for REE extraction/chromatography. (rocha2024rareearthelements pages 2-5, rocha2024rareearthelements pages 5-6)
Rocha et al. (2024) highlight the development of REE biosensors using REE-binding proteins, with potential mining and medical applications; examples include sensors with low-μM KD that can yield ~15-fold fluorescence increases (LanTERN) and other sensors detecting low-nM terbium in acid mine drainage (as summarized in the review). (rocha2024rareearthelements pages 6-8)
The same review describes selective precipitation of REEs with PQQ, noting that PQQ–REE complexes are practically insoluble such that adding PQQ can precipitate REEs from solution. (rocha2024rareearthelements pages 6-8)
Based on AM1 genetics/physiology and biochemical consensus, the most defensible primary annotation for moxF/mxaF (P16027) is:
- Function: catalytic large subunit of MxaFI-type methanol dehydrogenase; oxidizes methanol → formaldehyde in the periplasm using PQQ and Ca2+, and transfers electrons to cytochrome cL (MxaG). (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 1-4)
MxaF is essential for methanol growth without lanthanides, but under La3+ conditions it can become dispensable because XoxF-type MDHs dominate, consistent with measured growth rates where ΔmxaF ≈ wild type in methanol + La3+. (good2016pyrroloquinolinequinoneethanol pages 3-5, roszczenkojasinska2020geneproductsand pages 6-7)
The MxaF/XoxF split is now treated as an entry point into broader metal biology: understanding the lanthanide switch, uptake, and storage in AM1 has become tightly linked to proposed solutions for REE recovery and sensing (biosensors, bioaccumulation, immobilized binders). (rocha2024rareearthelements pages 1-2, rocha2024rareearthelements pages 5-6)
The following table consolidates the key functional-annotation facts and quantitative evidence.
| Feature | Annotation / evidence |
|---|---|
| Target identity | mxaF / moxF, UniProt P16027, locus MexAM1_META1p4538; encodes the large subunit of the canonical methanol dehydrogenase in Methylorubrum extorquens AM1. Roszczenko-Jasińska et al. explicitly map mxaF = MexAM1_META1p4538 in AM1. (roszczenkojasinska2020geneproductsand pages 4-5) |
| Enzyme name / EC | Methanol dehydrogenase [cytochrome c] large subunit MxaF; part of MxaFI-type MeDH; EC 1.1.2.7 per UniProt target definition. Literature describes MxaFI as the classical Ca²⁺-dependent methanol dehydrogenase of Gram-negative methylotrophs. (chu2016xoxfactsas pages 1-5, good2016pyrroloquinolinequinoneethanol pages 3-5) |
| Primary reaction | Catalyzes methanol oxidation to formaldehyde in methylotrophy; in AM1, when lanthanides are absent, MxaFI is the sole methanol oxidizer. (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 1-4) |
| Cofactors | PQQ-dependent quinoprotein with Ca²⁺ in the active site for MxaFI-type enzymes; contrasts with XoxF enzymes, which use lanthanides instead of Ca²⁺. (good2016pyrroloquinolinequinoneethanol pages 3-5, chu2016xoxfactsas pages 1-5, deng2018structureandfunction pages 7-10) |
| Subunit composition | MxaFI is an α2β2 heterotetramer composed of large subunit MxaF and small subunit MxaI. (good2016pyrroloquinolinequinoneethanol pages 3-5) |
| Cellular localization | MxaFI-type MDH is a soluble periplasmic enzyme; methanol oxidation in AM1 occurs in the periplasm. (good2016pyrroloquinolinequinoneethanol pages 3-5, chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 1-4) |
| Electron acceptor | The mxa operon includes mxaG, encoding the associated cytochrome cL electron acceptor; methylotrophic PQQ-ADHs in AM1 pair with cytochrome cL homologs. (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 1-4) |
| Operon / accessory partners | The AM1 mxa operon is reported as mxaFJGIRSACKLDEHB; associated factors include mxaI (small subunit), mxaG (cytochrome cL), mxaJ (periplasmic binding/chaperone-like factor), and proteins for Ca²⁺ insertion / MxaFI maturation (e.g., mxaACKL). Regulation involves MxcQE, MxbDM, and MxaB. (chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5) |
| Relationship to XoxF / lanthanide switch | AM1 contains one MxaFI-type MDH and two XoxF-type MDHs. In the absence of lanthanides, MxaFI supports methanol growth; in the presence of lanthanides, the “lanthanide switch” represses mxa genes and induces xox genes, shifting oxidation toward XoxF. XoxF1/XoxF2 also contribute to expression/regulation of the Ca²⁺-dependent MxaFI system. (good2016pyrroloquinolinequinoneethanol pages 3-5, chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5) |
| Promoter-reporter response to La³⁺ | In AM1 promoter fusions, mxa promoter signal fell from ~323 ± 63 RFU/OD600 in MeOH-only medium to ~61 ± 10 with 2 μM La³⁺, while xox1 rose from ~44 ± 3 to ~206 ± 11, directly illustrating the lanthanide switch. (roszczenkojasinska2020geneproductsand pages 7-10) |
| Growth phenotypes with La³⁺ | In MeOH + La³⁺, wild type and ΔmxaF both grew at 0.16 ± 0.01 h⁻¹; ΔxoxF1 dropped to 0.07 ± 0.00 h⁻¹ after a 6–9 h lag; ΔxoxF1 ΔxoxF2 and ΔmxaF ΔxoxF1 ΔxoxF2 grew only at ~0.04 h⁻¹ with a 6 h lag, showing that under La³⁺ conditions XoxF, not MxaF, is the major MDH system. (roszczenkojasinska2020geneproductsand pages 6-7, roszczenkojasinska2020geneproductsand media fa5edca9) |
| System-level effect of lanthanides on methanol growth | During lanthanide-dependent growth of AM1, growth on methanol is reported to be 15–22% faster with 10–12.5% higher yield than calcium-dependent growth, indicating more efficient Ln-supported methylotrophy overall; these gains are attributed mainly to XoxF1/ExaF rather than MxaF itself. (good2018investigationoflanthanidedependent pages 1-5) |
| Functional interpretation for annotation | MxaF is the catalytic large subunit of the classical Ca²⁺/PQQ-dependent, periplasmic methanol dehydrogenase that oxidizes methanol to formaldehyde and transfers electrons to cytochrome cL (MxaG). It is the principal methanol oxidation system without lanthanides, but is transcriptionally and physiologically downshifted when La³⁺/other lanthanides trigger use of XoxF-type enzymes. (good2016pyrroloquinolinequinoneethanol pages 3-5, chu2016xoxfactsas pages 1-5, roszczenkojasinska2020geneproductsand pages 4-5, roszczenkojasinska2020geneproductsand pages 7-10, roszczenkojasinska2020geneproductsand pages 6-7) |
Table: This table summarizes the core functional annotation for Methylorubrum extorquens AM1 mxaF/moxF (UniProt P16027), including biochemical role, localization, partners, and quantitative evidence for lanthanide-dependent regulation. It is useful as a compact evidence-backed reference for gene function and pathway context.
This report provides strong evidence for reaction, cofactors, subunit composition, localization, electron acceptor coupling, regulation, and quantitative growth/regulatory phenotypes in AM1. However, AM1-specific purified-enzyme kinetic constants and substrate panel data for MxaFI/MxaF were not present in the retrieved full texts; therefore, detailed kinetic/substrate specificity beyond methanol oxidation is not asserted here.
References
(roszczenkojasinska2020geneproductsand pages 4-5): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 92 citations and is from a peer-reviewed journal.
(good2016pyrroloquinolinequinoneethanol pages 3-5): Nathan M. Good, Huong N. Vu, Carly J. Suriano, Gabriel A. Subuyuj, Elizabeth Skovran, and N. Cecilia Martinez-Gomez. Pyrroloquinoline quinone ethanol dehydrogenase in methylobacterium extorquens am1 extends lanthanide-dependent metabolism to multicarbon substrates. Journal of Bacteriology, 198:3109-3118, Nov 2016. URL: https://doi.org/10.1128/jb.00478-16, doi:10.1128/jb.00478-16. This article has 154 citations and is from a peer-reviewed journal.
(chu2016xoxfactsas pages 1-5): Frances Chu and Mary E. Lidstrom. Xoxf acts as the predominant methanol dehydrogenase in the type i methanotroph methylomicrobium buryatense. Journal of Bacteriology, 198:1317-1325, Apr 2016. URL: https://doi.org/10.1128/jb.00959-15, doi:10.1128/jb.00959-15. This article has 194 citations and is from a peer-reviewed journal.
(deng2018structureandfunction pages 7-10): Yue Wen Deng, Soo Y. Ro, and Amy C. Rosenzweig. Structure and function of the lanthanide-dependent methanol dehydrogenase xoxf from the methanotroph methylomicrobium buryatense 5gb1c. JBIC Journal of Biological Inorganic Chemistry, 23:1037-1047, Aug 2018. URL: https://doi.org/10.1007/s00775-018-1604-2, doi:10.1007/s00775-018-1604-2. This article has 87 citations.
(roszczenkojasinska2020geneproductsand pages 1-4): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 92 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 7-10): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 92 citations and is from a peer-reviewed journal.
(good2018investigationoflanthanidedependent pages 8-12): Nathan M. Good, Olivia N. Walser, Riley S. Moore, Carly J. Suriano, Anna F. Huff, and N. Cecilia Martínez-Gómez. Investigation of lanthanide-dependent methylotrophy uncovers complementary roles for alcohol dehydrogenase enzymes. bioRxiv, May 2018. URL: https://doi.org/10.1101/329011, doi:10.1101/329011. This article has 23 citations.
(good2016pyrroloquinolinequinoneethanol pages 5-7): Nathan M. Good, Huong N. Vu, Carly J. Suriano, Gabriel A. Subuyuj, Elizabeth Skovran, and N. Cecilia Martinez-Gomez. Pyrroloquinoline quinone ethanol dehydrogenase in methylobacterium extorquens am1 extends lanthanide-dependent metabolism to multicarbon substrates. Journal of Bacteriology, 198:3109-3118, Nov 2016. URL: https://doi.org/10.1128/jb.00478-16, doi:10.1128/jb.00478-16. This article has 154 citations and is from a peer-reviewed journal.
(rocha2024rareearthelements pages 2-5): Raquel A. Rocha, Kirill Alexandrov, and Colin Scott. Rare earth elements in biology: from biochemical curiosity to solutions for extractive industries. Microbial Biotechnology, Jun 2024. URL: https://doi.org/10.1111/1751-7915.14503, doi:10.1111/1751-7915.14503. This article has 24 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand pages 6-7): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 92 citations and is from a peer-reviewed journal.
(roszczenkojasinska2020geneproductsand media fa5edca9): Paula Roszczenko-Jasińska, Huong N. Vu, Gabriel A. Subuyuj, Ralph Valentine Crisostomo, James Cai, Nicholas F. Lien, Erik J. Clippard, Elena M. Ayala, Richard T. Ngo, Fauna Yarza, Justin P. Wingett, Charumathi Raghuraman, Caitlin A. Hoeber, Norma C. Martinez-Gomez, and Elizabeth Skovran. Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in methylorubrum extorquens am1. Scientific Reports, Jul 2020. URL: https://doi.org/10.1038/s41598-020-69401-4, doi:10.1038/s41598-020-69401-4. This article has 92 citations and is from a peer-reviewed journal.
(good2018investigationoflanthanidedependent pages 1-5): Nathan M. Good, Olivia N. Walser, Riley S. Moore, Carly J. Suriano, Anna F. Huff, and N. Cecilia Martínez-Gómez. Investigation of lanthanide-dependent methylotrophy uncovers complementary roles for alcohol dehydrogenase enzymes. bioRxiv, May 2018. URL: https://doi.org/10.1101/329011, doi:10.1101/329011. This article has 23 citations.
(rocha2024rareearthelements pages 1-2): Raquel A. Rocha, Kirill Alexandrov, and Colin Scott. Rare earth elements in biology: from biochemical curiosity to solutions for extractive industries. Microbial Biotechnology, Jun 2024. URL: https://doi.org/10.1111/1751-7915.14503, doi:10.1111/1751-7915.14503. This article has 24 citations and is from a peer-reviewed journal.
(rocha2024rareearthelements pages 5-6): Raquel A. Rocha, Kirill Alexandrov, and Colin Scott. Rare earth elements in biology: from biochemical curiosity to solutions for extractive industries. Microbial Biotechnology, Jun 2024. URL: https://doi.org/10.1111/1751-7915.14503, doi:10.1111/1751-7915.14503. This article has 24 citations and is from a peer-reviewed journal.
(rocha2024rareearthelements pages 6-8): Raquel A. Rocha, Kirill Alexandrov, and Colin Scott. Rare earth elements in biology: from biochemical curiosity to solutions for extractive industries. Microbial Biotechnology, Jun 2024. URL: https://doi.org/10.1111/1751-7915.14503, doi:10.1111/1751-7915.14503. This article has 24 citations and is from a peer-reviewed journal.