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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 Protein MoxJ (precursor) encoded by moxJ (synonym mxaJ) from Methylorubrum extorquens strain AM1 (formerly Methylobacterium extorquens AM1), UniProt P16028. In the accessible literature, mxaJ/moxJ is consistently discussed as an accessory gene within the canonical mxa methanol-oxidation operon (mxaFJGIRSACKLDEHB), adjacent to the catalytic MDH subunit gene mxaF and the cytochrome electron-acceptor gene mxaG, matching the UniProt context provided. (goodwin1995thebiosynthesisof pages 5-7, goodwin1995thebiosynthesisof pages 4-5, schmidt2010functionalinvestigationof pages 37-39)
In M. extorquens AM1, methylotrophic growth begins with periplasmic oxidation of methanol, classically by PQQ-dependent methanol dehydrogenase (MDH) (MxaFI), transferring electrons to a periplasmic cytochrome cL (MxaG). The mxa operon encodes not only catalytic subunits but also accessory proteins required for MDH biogenesis and function in the periplasm. (goodwin1995thebiosynthesisof pages 4-5, schmidt2010functionalinvestigationof pages 39-45)
Historically, MxaJ was described as a predicted ~30 kDa periplasmic precursor protein with uncertain role, proposed either as a third MDH subunit or a molecular chaperone required for assembly/optimal in vivo function of MDH. (goodwin1995thebiosynthesisof pages 4-5, goodwin1995thebiosynthesisof pages 5-7)
A later comparative genomic/protein-family interpretation classifies MxaJ/XoxJ-like proteins as Family 3 extracellular solute-binding proteins (COG0834; Pfam family reported in that context), suggesting a solute-binding-protein-like fold and raising hypotheses such as binding methanol or facilitating formaldehyde release/detoxification (hypotheses; not direct AM1 biochemical proof). (wu2015xoxftypemethanoldehydrogenase pages 8-12)
Periplasmic localization is supported by: (i) prediction that mxaJ encodes a periplasmic precursor protein; and (ii) the broader model that MDH structural gene products carry signal sequences that are cleaved upon translocation to the periplasm, where PQQ/haem-containing complexes assemble. (goodwin1995thebiosynthesisof pages 4-5, goodwin1995thebiosynthesisof pages 5-7)
Export pathway (Tat vs Sec): the accessible papers used here support periplasmic export but do not directly determine whether AM1 MoxJ uses Tat vs Sec machinery; thus, Tat assignment (even if present in UniProt features) should be treated as database-based unless validated by targeted experiments. (goodwin1995thebiosynthesisof pages 4-5)
The strongest mechanistic evidence currently available in the retrieved corpus is that MxaJ is an MDH assembly chaperone that mediates PQQ incorporation into the catalytic subunit MxaF. Zhou et al. (Nature Communications, 2025-07, https://doi.org/10.1038/s41467-025-61958-w) reconstructed an MDH assembly system and captured intermediate complexes, concluding that:
- MxaJ forms an MxaF/MxaJ complex and promotes conformational changes enabling PQQ entry/incorporation.
- After PQQ binding, MxaI engagement promotes MxaJ release, yielding mature PQQ-loaded MxaF/MxaI complexes.
This provides a direct biochemical/structural basis for the long-standing “assembly protein / periplasmic chaperone” hypothesis for MxaJ-family proteins. (zhou2025decipheringtheassembly pages 4-5, zhou2025decipheringtheassembly pages 1-2)
Genomic context places mxaJ directly adjacent to mxaF and mxaG within the mxa cluster, which encodes the periplasmic methanol oxidation module. This operon architecture supports a role for MxaJ in the biogenesis/activation of the periplasmic MDH system rather than downstream cytosolic C1 assimilation. (schmidt2010functionalinvestigationof pages 39-45, goodwin1995thebiosynthesisof pages 5-7)
Direct physical interactions of AM1 MxaJ with MxaG or the assembled MDH complex are not demonstrated in the accessible AM1-specific primary evidence here; however, related systems and models depict periplasmic co-assembly of exported proteins with cofactors. (goodwin1995thebiosynthesisof media 8f8bf987, goodwin1995thebiosynthesisof pages 4-5)
In M. extorquens AM1, lanthanides (e.g., La3+) induce a regulatory “lanthanide switch” favoring lanthanide-dependent alcohol dehydrogenases (Xox systems) and repressing the Ca-dependent mxa system.
RNA-seq under methanol growth with 2 µM La3+ (FDR < 0.15; |log2FC| > 1) shows mxaJ is strongly downregulated (log2FC = −7.5, p = 2.00E−18), together with other mxa genes (e.g., mxaF −8.0; mxaG −7.4). (Scientific Reports, 2019-03, https://doi.org/10.1038/s41598-019-41043-1) (good2019contrastinginvitro pages 7-8)
In the same dataset, the xox1 locus (including xoxJ, an MxaJ-like homolog) is upregulated in the presence of La3+ (reported ~16–21-fold; with example log2 values: xoxJ ~ 4.0). (good2019contrastinginvitro pages 6-7)
Although direct AM1 mxaJ knockout phenotype data were not retrieved here, xoxJ (MxaJ-like homolog) mutants show strong growth impairments under methanol + La3+ conditions in AM1: for example, one dataset reports xoxJ growth at 0.04 ± 0.01 h−1 on methanol + La3+ with a long lag, compared with higher rates on methanol without La3+. (Scientific Reports, 2020-07, https://doi.org/10.1038/s41598-020-69401-4) (roszczenkojasinska2020geneproductsand pages 6-7)
This supports functional importance of MxaJ-like proteins across alternative periplasmic PQQ-ADH modules, consistent with a conserved maturation/activation role. (roszczenkojasinska2020geneproductsand pages 4-5)
A separate AM1 study reports that adding lanthanum increases methanol-growth rate by ~9–12%, consistent with a switch to lanthanide-dependent periplasmic dehydrogenases while repressing the mxa system. (Scientific Reports, 2019-03, https://doi.org/10.1038/s41598-019-41043-1) (good2019contrastinginvitro pages 1-2)
Older biochemical/genetic synthesis notes predict an MxaJ precursor of ~30 kDa, and report isolation of a ~32 kDa protein in a related methylotroph whose N-terminus matched the predicted mxaJ product, supporting that MxaJ-family proteins are small exported periplasmic factors. (Microbiology, 1995-05, https://doi.org/10.1099/13500872-141-5-1051) (goodwin1995thebiosynthesisof pages 5-7)
Direct 2023–2024 AM1-specific mechanistic studies of MoxJ/MxaJ were not retrieved in the accessible corpus. However, multiple 2024 results strongly update the context for MxaJ-like proteins in methanol oxidation systems:
A 2024 metagenomics study of weathered granite/soils found that lanthanide-dependent XoxF-type methanol dehydrogenase systems are widespread and that XoxF gene clusters commonly include accessory/electron-transfer genes such as xoxJ and xoxG (MxaJ/MxaG homologs), indicating that MxaJ-like accessory proteins are broadly conserved features of periplasmic PQQ-ADH methanol-oxidation modules in nature. (BMC Biology, 2024-02, https://doi.org/10.1186/s12915-024-01841-0) (voutsinos2024weatheredgranitesand pages 4-7, voutsinos2024weatheredgranitesand pages 1-2)
The same 2024 work reports lanthanide concentrations across weathering gradients (e.g., 427 ppm in lightly weathered granite declining to 214 ppm in highly weathered granite and 80 ppm in soil) and recovers 411 XoxF-type MDH sequences (dominated by XoxF3) while not detecting Ca-dependent MxaF sequences in the reconstructed genomes. These data strengthen the view that lanthanide-dependent PQQ-ADH systems (with accessory xoxJ) can be ecologically dominant. (voutsinos2024weatheredgranitesand pages 7-10, voutsinos2024weatheredgranitesand pages 2-4)
M. extorquens AM1 is widely used as a platform methylotroph for C1-based biotechnological approaches. Efficient methanol oxidation depends on functional periplasmic PQQ-ADH systems. Because MxaJ is now mechanistically linked to PQQ incorporation into MxaF (a key maturation step), it is a credible engineering target for:
- heterologous reconstruction of active MDH systems,
- improving robustness of methanol oxidation modules,
- enabling controlled switching between Ca-dependent and lanthanide-dependent pathways (via xoxJ-like modules).
This application logic is specifically supported by the demonstration that MxaJ enables PQQ loading during MDH maturation (reconstructed in a heterologous system). (zhou2025decipheringtheassembly pages 1-2)
Goodwin & Anthony (Microbiology, 1995-05, https://doi.org/10.1099/13500872-141-5-1051) summarize evidence and propose two models: MxaJ as a component (“third subunit”) of MDH, or as a molecular chaperone essential for assembly of active MDH; they did not resolve which model is correct at the time. (goodwin1995thebiosynthesisof pages 4-5)
Zhou et al. (Nature Communications, 2025-07, https://doi.org/10.1038/s41467-025-61958-w) provide direct structural and mechanistic evidence supporting the chaperone-mediated PQQ incorporation model, resolving a long-standing question about MxaJ-family proteins. (zhou2025decipheringtheassembly pages 4-5, zhou2025decipheringtheassembly pages 1-2)
Goodwin & Anthony provide an operon/assembly model figure showing exported preproteins and periplasmic assembly of the methanol-oxidation module including the mxaFJGI region; cropped figure/table images were retrieved from that paper. (goodwin1995thebiosynthesisof media 8f8bf987, goodwin1995thebiosynthesisof media 3fbdfcda, goodwin1995thebiosynthesisof media 440826dc, goodwin1995thebiosynthesisof media 75627ce3)
| Feature | Evidence summary | Key citations (with year) |
|---|---|---|
| Gene names / target identity | The literature for Methylorubrum/Methylobacterium extorquens AM1 uses mxaJ and moxJ for the same methanol-oxidation accessory gene in the canonical mxa cluster; Schmidt et al. discuss MxaJ and its paralog XoxJ in analogous loci, supporting that UniProt P16028 corresponds to the AM1 methanol-oxidation accessory protein rather than an unrelated gene symbol in another organism. | Goodwin & Anthony 1995 (goodwin1995thebiosynthesisof pages 5-7, goodwin1995thebiosynthesisof pages 4-5); Schmidt et al. 2010 (schmidt2010functionalinvestigationof pages 37-39, schmidt2010functionalinvestigationof pages 87-92, schmidt2010functionalinvestigationof pages 39-45) |
| Operon / pathway context | mxaJ is located in the mxaF-mxaJ-mxaG-mxaI region within the larger methanol-oxidation operon (mxaFJGIRSACKLDEHB). This places MxaJ directly alongside the catalytic MDH subunits (MxaF/MxaI) and the electron acceptor cytochrome cL (MxaG), consistent with a role in MDH biogenesis or function in periplasmic methanol oxidation. | Goodwin & Anthony 1995 (goodwin1995thebiosynthesisof pages 5-7, goodwin1995thebiosynthesisof pages 4-5, goodwin1995thebiosynthesisof media 8f8bf987); Schmidt et al. 2010 (schmidt2010functionalinvestigationof pages 37-39, schmidt2010functionalinvestigationof pages 87-92, schmidt2010functionalinvestigationof pages 39-45) |
| Predicted localization / export | Goodwin & Anthony describe mxaJ as encoding a precursor of a periplasmic protein and state that structural-gene products carry signal sequences cleaved upon translocation to the periplasm. Figure/model context shows preproteins entering the periplasm for assembly. The available snippets do not directly establish whether MxaJ uses Tat versus Sec export, so export-pathway assignment remains uncertain from the provided literature evidence alone. | Goodwin & Anthony 1995 (goodwin1995thebiosynthesisof pages 5-7, goodwin1995thebiosynthesisof pages 4-5, goodwin1995thebiosynthesisof media 8f8bf987) |
| Molecular weight | Historical review evidence describes the predicted MxaJ precursor as ~30 kDa; a ~32 kDa protein isolated from Acetobacter methanolicus had an N-terminus matching the predicted mxaJ product, supporting a small exported accessory-protein assignment. | Goodwin & Anthony 1995 (goodwin1995thebiosynthesisof pages 5-7) |
| Domain / family assignment | Older review literature reported no significant homology to known proteins at that time, but later sequence analysis classified MxaJ/XoxJ-like proteins as Family 3 extracellular solute-binding proteins. This aligns broadly with modern database/domain assignments of MoxJ/MxaJ as a solute-binding-protein-like accessory factor, although the provided snippets do not directly test ligand binding. | Goodwin & Anthony 1995 (goodwin1995thebiosynthesisof pages 4-5); Wu et al. 2015 (wu2015xoxftypemethanoldehydrogenase pages 8-12) |
| Proposed function (historical view) | Before direct structural evidence, MxaJ was proposed either as a third subunit of methanol dehydrogenase or as a molecular chaperone / assembly protein required for formation or optimal in vivo function of MDH. Schmidt et al. reiterate that MxaJ/XoxJ had been suggested to be an assembly protein or periplasmic chaperone. | Goodwin & Anthony 1995 (goodwin1995thebiosynthesisof pages 5-7, goodwin1995thebiosynthesisof pages 4-5); Schmidt et al. 2010 (schmidt2010functionalinvestigationof pages 37-39, schmidt2010functionalinvestigationof pages 87-92, schmidt2010functionalinvestigationof pages 39-45) |
| Current mechanistic understanding | Recent structural work shows MxaJ functions as an MDH assembly chaperone: it binds folded MxaF, forms an MxaF/MxaJ intermediate, and promotes PQQ incorporation during MDH maturation. After PQQ loading, MxaI engages and helps displace MxaJ, yielding mature PQQ-loaded MxaF/MxaI. This is the strongest currently available mechanistic evidence in the provided set. | Zhou et al. 2025 (zhou2025decipheringtheassembly pages 4-5, zhou2025decipheringtheassembly pages 1-2) |
| Relation to XoxJ / ExaJ paralogs | AM1 and related methylotrophs often encode xoxJ/exaJ homologs next to alternative alcohol dehydrogenase genes. Roszczenko-Jasińska et al. note that xoxF/exaF loci often contain mxaJ homologs, while Schmidt et al. describe xoxJ as corresponding to the putative periplasmic chaperone/assembly role of MxaJ. This supports a conserved accessory role across Ca-dependent and lanthanide-associated MDH-like systems. | Schmidt et al. 2010 (schmidt2010functionalinvestigationof pages 87-92, schmidt2010functionalinvestigationof pages 39-45); Roszczenko-Jasińska et al. 2020 (schmidt2010functionalinvestigationof pages 37-39) |
| Evidence gaps / uncertainty | The provided snippets do not supply clear AM1-specific mxaJ knockout phenotype data, direct biochemical measurements of MxaJ interaction with MxaG, or direct demonstration of Tat export for AM1 MxaJ. Thus, periplasmic accessory/chaperone function is well supported, but some annotation details remain inferential or await more direct AM1-specific experiments in the accessible evidence set. | Goodwin & Anthony 1995 (goodwin1995thebiosynthesisof pages 5-7, goodwin1995thebiosynthesisof pages 4-5); Schmidt et al. 2010 (schmidt2010functionalinvestigationof pages 87-92, schmidt2010functionalinvestigationof pages 39-45); Zhou et al. 2025 (zhou2025decipheringtheassembly pages 1-2) |
Table: This table condenses the evidence-supported functional annotation for MoxJ/MxaJ (UniProt P16028) in Methylorubrum extorquens AM1. It highlights what is directly supported by the cited literature and explicitly marks remaining evidence gaps such as export-pathway uncertainty and limited AM1-specific mutant data.
References
(goodwin1995thebiosynthesisof pages 5-7): Pat M. Goodwin and Christopher Anthony. The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria. Microbiology, 141 ( Pt 5):1051-64, May 1995. URL: https://doi.org/10.1099/13500872-141-5-1051, doi:10.1099/13500872-141-5-1051. This article has 39 citations and is from a peer-reviewed journal.
(goodwin1995thebiosynthesisof pages 4-5): Pat M. Goodwin and Christopher Anthony. The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria. Microbiology, 141 ( Pt 5):1051-64, May 1995. URL: https://doi.org/10.1099/13500872-141-5-1051, doi:10.1099/13500872-141-5-1051. This article has 39 citations and is from a peer-reviewed journal.
(schmidt2010functionalinvestigationof pages 37-39): Sabrina Schmidt, Philipp Christen, Patrick Kiefer, and Julia A. Vorholt. Functional investigation of methanol dehydrogenase-like protein xoxf in methylobacterium extorquens am1. Microbiology, 156 Pt 8:2575-86, Aug 2010. URL: https://doi.org/10.1099/mic.0.038570-0, doi:10.1099/mic.0.038570-0. This article has 141 citations and is from a peer-reviewed journal.
(schmidt2010functionalinvestigationof pages 39-45): Sabrina Schmidt, Philipp Christen, Patrick Kiefer, and Julia A. Vorholt. Functional investigation of methanol dehydrogenase-like protein xoxf in methylobacterium extorquens am1. Microbiology, 156 Pt 8:2575-86, Aug 2010. URL: https://doi.org/10.1099/mic.0.038570-0, doi:10.1099/mic.0.038570-0. This article has 141 citations and is from a peer-reviewed journal.
(wu2015xoxftypemethanoldehydrogenase pages 8-12): Ming L. Wu, Hans J. C. T. Wessels, Arjan Pol, Huub J. M. Op den Camp, Mike S. M. Jetten, Laura van Niftrik, and Jan T. Keltjens. Xoxf-type methanol dehydrogenase from the anaerobic methanotroph “candidatus methylomirabilis oxyfera”. Applied and Environmental Microbiology, 81:1442-1451, Feb 2015. URL: https://doi.org/10.1128/aem.03292-14, doi:10.1128/aem.03292-14. This article has 81 citations and is from a peer-reviewed journal.
(zhou2025decipheringtheassembly pages 4-5): Haichuan Zhou, Junqing Sun, Jian Cheng, Min Wu, Jie Bai, Qian Li, Jie Shen, Manman Han, Chen Yang, Liangpo Li, Yuwan Liu, Qichen Cao, Weidong Liu, Haixia Xiao, Hongjun Dong, Feng Gao, and Huifeng Jiang. Deciphering the assembly process of pqq dependent methanol dehydrogenase. Nature Communications, Jul 2025. URL: https://doi.org/10.1038/s41467-025-61958-w, doi:10.1038/s41467-025-61958-w. This article has 6 citations and is from a highest quality peer-reviewed journal.
(zhou2025decipheringtheassembly pages 1-2): Haichuan Zhou, Junqing Sun, Jian Cheng, Min Wu, Jie Bai, Qian Li, Jie Shen, Manman Han, Chen Yang, Liangpo Li, Yuwan Liu, Qichen Cao, Weidong Liu, Haixia Xiao, Hongjun Dong, Feng Gao, and Huifeng Jiang. Deciphering the assembly process of pqq dependent methanol dehydrogenase. Nature Communications, Jul 2025. URL: https://doi.org/10.1038/s41467-025-61958-w, doi:10.1038/s41467-025-61958-w. This article has 6 citations and is from a highest quality peer-reviewed journal.
(goodwin1995thebiosynthesisof media 8f8bf987): Pat M. Goodwin and Christopher Anthony. The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria. Microbiology, 141 ( Pt 5):1051-64, May 1995. URL: https://doi.org/10.1099/13500872-141-5-1051, doi:10.1099/13500872-141-5-1051. This article has 39 citations and is from a peer-reviewed journal.
(good2019contrastinginvitro pages 7-8): Nathan M. Good, Riley S. Moore, Carly J. Suriano, and N. Cecilia Martinez-Gomez. Contrasting in vitro and in vivo methanol oxidation activities of lanthanide-dependent alcohol dehydrogenases xoxf1 and exaf from methylobacterium extorquens am1. Scientific Reports, Mar 2019. URL: https://doi.org/10.1038/s41598-019-41043-1, doi:10.1038/s41598-019-41043-1. This article has 92 citations and is from a peer-reviewed journal.
(good2019contrastinginvitro pages 6-7): Nathan M. Good, Riley S. Moore, Carly J. Suriano, and N. Cecilia Martinez-Gomez. Contrasting in vitro and in vivo methanol oxidation activities of lanthanide-dependent alcohol dehydrogenases xoxf1 and exaf from methylobacterium extorquens am1. Scientific Reports, Mar 2019. URL: https://doi.org/10.1038/s41598-019-41043-1, doi:10.1038/s41598-019-41043-1. This article has 92 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 98 citations and is from a peer-reviewed journal.
(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 98 citations and is from a peer-reviewed journal.
(good2019contrastinginvitro pages 1-2): Nathan M. Good, Riley S. Moore, Carly J. Suriano, and N. Cecilia Martinez-Gomez. Contrasting in vitro and in vivo methanol oxidation activities of lanthanide-dependent alcohol dehydrogenases xoxf1 and exaf from methylobacterium extorquens am1. Scientific Reports, Mar 2019. URL: https://doi.org/10.1038/s41598-019-41043-1, doi:10.1038/s41598-019-41043-1. This article has 92 citations and is from a peer-reviewed journal.
(voutsinos2024weatheredgranitesand pages 4-7): Marcos Y. Voutsinos, Jacob A. West-Roberts, Rohan Sachdeva, John W. Moreau, and Jillian F. Banfield. Weathered granites and soils harbour microbes with lanthanide-dependent methylotrophic enzymes. BMC Biology, Feb 2024. URL: https://doi.org/10.1186/s12915-024-01841-0, doi:10.1186/s12915-024-01841-0. This article has 13 citations and is from a domain leading peer-reviewed journal.
(voutsinos2024weatheredgranitesand pages 1-2): Marcos Y. Voutsinos, Jacob A. West-Roberts, Rohan Sachdeva, John W. Moreau, and Jillian F. Banfield. Weathered granites and soils harbour microbes with lanthanide-dependent methylotrophic enzymes. BMC Biology, Feb 2024. URL: https://doi.org/10.1186/s12915-024-01841-0, doi:10.1186/s12915-024-01841-0. This article has 13 citations and is from a domain leading peer-reviewed journal.
(voutsinos2024weatheredgranitesand pages 7-10): Marcos Y. Voutsinos, Jacob A. West-Roberts, Rohan Sachdeva, John W. Moreau, and Jillian F. Banfield. Weathered granites and soils harbour microbes with lanthanide-dependent methylotrophic enzymes. BMC Biology, Feb 2024. URL: https://doi.org/10.1186/s12915-024-01841-0, doi:10.1186/s12915-024-01841-0. This article has 13 citations and is from a domain leading peer-reviewed journal.
(voutsinos2024weatheredgranitesand pages 2-4): Marcos Y. Voutsinos, Jacob A. West-Roberts, Rohan Sachdeva, John W. Moreau, and Jillian F. Banfield. Weathered granites and soils harbour microbes with lanthanide-dependent methylotrophic enzymes. BMC Biology, Feb 2024. URL: https://doi.org/10.1186/s12915-024-01841-0, doi:10.1186/s12915-024-01841-0. This article has 13 citations and is from a domain leading peer-reviewed journal.
(goodwin1995thebiosynthesisof media 3fbdfcda): Pat M. Goodwin and Christopher Anthony. The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria. Microbiology, 141 ( Pt 5):1051-64, May 1995. URL: https://doi.org/10.1099/13500872-141-5-1051, doi:10.1099/13500872-141-5-1051. This article has 39 citations and is from a peer-reviewed journal.
(goodwin1995thebiosynthesisof media 440826dc): Pat M. Goodwin and Christopher Anthony. The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria. Microbiology, 141 ( Pt 5):1051-64, May 1995. URL: https://doi.org/10.1099/13500872-141-5-1051, doi:10.1099/13500872-141-5-1051. This article has 39 citations and is from a peer-reviewed journal.
(goodwin1995thebiosynthesisof media 75627ce3): Pat M. Goodwin and Christopher Anthony. The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria. Microbiology, 141 ( Pt 5):1051-64, May 1995. URL: https://doi.org/10.1099/13500872-141-5-1051, doi:10.1099/13500872-141-5-1051. This article has 39 citations and is from a peer-reviewed journal.
(schmidt2010functionalinvestigationof pages 87-92): Sabrina Schmidt, Philipp Christen, Patrick Kiefer, and Julia A. Vorholt. Functional investigation of methanol dehydrogenase-like protein xoxf in methylobacterium extorquens am1. Microbiology, 156 Pt 8:2575-86, Aug 2010. URL: https://doi.org/10.1099/mic.0.038570-0, doi:10.1099/mic.0.038570-0. This article has 141 citations and is from a peer-reviewed journal.
(schmidt2010functionalinvestigationof pages 61-66): Sabrina Schmidt, Philipp Christen, Patrick Kiefer, and Julia A. Vorholt. Functional investigation of methanol dehydrogenase-like protein xoxf in methylobacterium extorquens am1. Microbiology, 156 Pt 8:2575-86, Aug 2010. URL: https://doi.org/10.1099/mic.0.038570-0, doi:10.1099/mic.0.038570-0. This article has 141 citations and is from a peer-reviewed journal.