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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 UniProt Q88NC0 is annotated as cyclic pyranopterin monophosphate (cPMP) synthase (EC 4.6.1.17) and as molybdenum cofactor (Moco) biosynthesis protein C (MoaC) in Pseudomonas putida KT2440. This matches the widely conserved bacterial MoaC-family enzyme function in the Moco biosynthesis pathway, where MoaC catalyzes conversion of the MoaA product (3′,8-cH2GTP) to cPMP. The literature retrieved here consistently uses MoaC in this sense and does not indicate a conflicting alternative gene/protein meaning for the symbol in bacteria. (leimkuhler2016bacterialmolybdoenzymesold pages 2-4, yokoyama2021resolvingthemultidecadelong pages 1-2)
Conclusion: The gene symbol moaC matches the UniProt description and known MoaC-family function; the organism context is aligned with bacterial MoaC biochemistry. (leimkuhler2016bacterialmolybdoenzymesold pages 2-4, yokoyama2021resolvingthemultidecadelong pages 1-2)
Moco is a molybdenum-containing cofactor required for catalytic activity of many molybdenum-dependent enzymes (molybdoenzymes). Conceptually, it consists of Mo complexed to a pterin scaffold; the pterin-only (metal-free) form is termed molybdopterin (MPT), and insertion of Mo into MPT yields the active Moco. (mendel2024thefinalstep pages 1-2, mendel2024thefinalstep pages 2-4)
Moco is generally chemically unstable outside of its protein environment, so in most organisms it must be synthesized de novo rather than acquired as a nutrient. (yokoyama2021resolvingthemultidecadelong pages 1-2)
Across bacteria and eukaryotes, Moco biosynthesis is commonly described as a sequence of conserved steps. A mechanistic perspective summarizes three conserved stages: (1) rearrangement of GTP into cPMP, (2) sulfur insertion to form MPT, and (3) insertion of molybdate (Mo) to produce Moco. (yokoyama2021resolvingthemultidecadelong pages 1-2, yokoyama2018radicalbreakthroughsin pages 3-4)
In bacteria, the first step (cPMP formation) is carried out by two proteins, MoaA and MoaC, where:
This MoaA→MoaC handoff is now considered the physiological sequence, revising older models that assigned most chemistry to MoaA and treated MoaC as noncatalytic. (yokoyama2018radicalbreakthroughsin pages 3-4, hover2013identificationofa pages 1-2)
MoaC catalyzes the conversion of the MoaA product, 3′,8-cH2GTP, into cyclic pyranopterin monophosphate (cPMP). (yokoyama2021resolvingthemultidecadelong pages 4-5, yokoyama2021resolvingthemultidecadelong pages 7-9, hover2013identificationofa pages 1-2)
This establishes MoaC’s substrate specificity as being directed to 3′,8-cH2GTP (not GTP directly) and its product as cPMP, the first stable committed intermediate in Moco biosynthesis. (yokoyama2021resolvingthemultidecadelong pages 4-5, yokoyama2021resolvingthemultidecadelong pages 1-2)
Available biochemical studies report that MoaC recognizes 3′,8-cH2GTP with very high apparent affinity:
These values support the interpretation that MoaC is tuned to efficiently capture/turn over the labile MoaA product in vivo. (yokoyama2018radicalbreakthroughsin pages 4-6)
A mechanistic/structural perspective reports that bacterial MoaC:
Crystal structures of E. coli MoaC bound to either 3′,8-cH2GTP or cPMP show both ligands in the same ligand-binding pocket and contacting the same residue set, and those residues are required for catalytic function in vitro/in vivo—supporting this pocket as the active site. (yokoyama2021resolvingthemultidecadelong pages 4-5)
Evidence indicates MoaC catalysis is coupled to protein conformational changes:
A proposed working mechanism assigns catalytic roles to residues including D128 (general base in a retro-aldol cleavage step) and K51/K131 (general acid/base catalysis during rearrangement/ring expansion), and argues that pyranopterin formation is coupled to cyclic phosphate formation rather than proceeding through a stable “pyranopterin triphosphate” intermediate. (yokoyama2018radicalbreakthroughsin pages 8-9)
Moco biosynthesis enables a broad family of molybdoenzymes. A 2024 review emphasizes that most characterized Mo-containing enzymes are bacterial and lists representative molybdoenzymes including formate dehydrogenase, nitrate reductase, DMSO reductase, xanthine dehydrogenase, and aldehyde oxidase. (mendel2024thefinalstep pages 1-2)
A widely cited bacterial review classifies bacterial molybdoenzymes into three major families and notes that prokaryotes possess all three families; it also states that 74% of bacteria representing almost all phyla utilize the molybdenum cofactor, and that some bacteria can encode very large molybdoproteomes (e.g., ~60 molybdoproteins in one example organism). (leimkuhler2016bacterialmolybdoenzymesold pages 1-2)
Implication for P. putida KT2440: While KT2440-specific molybdoproteome/phenotype data were not retrieved here for PP_1292/moaC specifically, the conserved role of MoaC in cPMP synthesis implies it is upstream of all KT2440 Moco-dependent enzymes, including potential nitrate-/formate-/S-oxide-related oxidoreductases, where present. (yokoyama2021resolvingthemultidecadelong pages 1-2, leimkuhler2016bacterialmolybdoenzymesold pages 1-2)
Direct experimental localization for P. putida KT2440 MoaC (Q88NC0) was not found in the retrieved corpus. However, MoaC is characterized biochemically and structurally as a soluble enzyme that binds small nucleotide-like substrates/products, consistent with an intracellular/cytosolic site of action for early cofactor biosynthesis. This is an inference from enzyme class and pathway context rather than a KT2440-specific localization experiment. (leimkuhler2016bacterialmolybdoenzymesold pages 2-4, yokoyama2021resolvingthemultidecadelong pages 7-9)
Regarding cellular organization/complex formation, a mechanistic perspective notes that in vivo interaction networks among MoaA, MoaC, MPT synthase, and sulfur-trafficking enzymes have been reported in Pseudomonas aeruginosa using GFP-PFCA, suggesting that (at least in some Pseudomonads) MoaC participates in a coordinated intracellular Moco-biosynthetic protein network rather than acting fully independently. (yokoyama2021resolvingthemultidecadelong pages 4-5)
A regulatory review highlights moa pathway regulation by describing the moaA mRNA leader as containing two CsrA-binding sites and constituting a MOCO-sensing riboswitch; it is described as “the first example of a riboswitch aptamer that interacts with two regulatory factors, a low-molecular-weight ligand and an RNA binding protein.” (seyll2013theribonucleoproteincsr pages 6-8)
This is directly about moaA, but it is relevant to functional annotation of moaC because MoaA and MoaC act sequentially in cPMP synthesis, and regulation of MoaA expression can functionally gate flux into the MoaC-catalyzed step. (yokoyama2021resolvingthemultidecadelong pages 1-2, seyll2013theribonucleoproteincsr pages 6-8)
Despite targeted searching, no primary study in the retrieved corpus directly reports genetic knockouts, phenotypes, operon structure, or expression fold-changes for P. putida KT2440 PP_1292/moaC. One retrieved source cites prior KT2440 transcriptome work under water stress, but the accessible text excerpt does not provide extractable moaC-specific quantitative results. (narihiro2016culturaltranscriptomicand pages 9-10)
Therefore, KT2440 functional annotation for Q88NC0 is currently best supported by strong conserved biochemical/structural evidence for MoaC function across bacteria plus Pseudomonas-context regulatory/network observations (mainly from P. aeruginosa and general bacterial studies), rather than KT2440-specific wet-lab characterization. (yokoyama2021resolvingthemultidecadelong pages 4-5, yokoyama2021resolvingthemultidecadelong pages 7-9, hover2013identificationofa pages 1-2)
A 2024 review focused on the final step of Moco biosynthesis (Mo insertion by Mo-insertase) reiterates modern consensus definitions of Moco (Mo complexed to a pterin scaffold) and emphasizes the breadth of Mo enzyme biology, noting that over 50 Mo-containing enzymes have been characterized and that the majority are bacterial. (Mendel & Oliphant, 2024; published Sep 2024; https://doi.org/10.3390/molecules29184458) (mendel2024thefinalstep pages 1-2)
Although this 2024 review is not MoaC-focused, it provides up-to-date framing of Moco enzyme importance and is relevant for contextualizing why MoaC (as an early biosynthetic enzyme) is biologically consequential. (mendel2024thefinalstep pages 1-2)
The most detailed MoaC mechanistic/structural insights in the retrieved set come from 2013–2021 work (identification of 3′,8-cH2GTP; hexameric assembly; loop gating; intermediate trapping). These constitute the current working mechanistic model and remain the core reference points for MoaC functional annotation. (hover2013identificationofa pages 1-2, yokoyama2021resolvingthemultidecadelong pages 7-9, yokoyama2018radicalbreakthroughsin pages 8-9)
A key recent trend in the field is the shift from “MoaA-only chemistry” models to a two-enzyme, handoff-based model where MoaC performs major rearrangement chemistry to build the pyranopterin. (yokoyama2018radicalbreakthroughsin pages 3-4, hover2013identificationofa pages 1-2)
While MoaC itself is a biosynthetic enzyme (not typically a direct industrial catalyst), its product (cPMP) enables bacterial molybdoenzymes with major real-world relevance:
Strong evidence (high confidence): Molecular function of MoaC as 3′,8-cH2GTP → cPMP synthase is supported by direct biochemical identification of the physiological substrate and product and by mechanistic/structural data (binding pocket, oligomerization, catalytic loop dynamics) from well-cited primary literature. This supports confident functional annotation of P. putida MoaC by homology. (hover2013identificationofa pages 1-2, yokoyama2021resolvingthemultidecadelong pages 7-9)
Moderate evidence: Participation in a coordinated “Moco biosynthesis interactome” is supported for Pseudomonas aeruginosa (not KT2440) and suggests a plausible analogous organization in P. putida, but this extrapolation should be treated as hypothesis pending KT2440-specific experiments. (yokoyama2021resolvingthemultidecadelong pages 4-5)
Weak/absent evidence (gap): KT2440-specific operon structure, regulation of moaC itself, phenotypes of moaC mutants, and direct subcellular localization have not been retrieved here; these are key items for a fully organism-specific functional annotation and are recommended targets for future investigation (e.g., targeted genetics and proteomics). (narihiro2016culturaltranscriptomicand pages 9-10)
The following table consolidates the main functional and mechanistic claims for MoaC, including quantitative kinetics and Pseudomonas-context notes.
| Claim/topic | Key details | Evidence type (biochem/structural/genetic/regulatory) | Organism/system | Source (author year journal) | DOI/URL | Context ID |
|---|---|---|---|---|---|---|
| Verified target family/function | UniProt Q88NC0 is annotated as MoaC/cyclic pyranopterin monophosphate synthase (EC 4.6.1.17), the canonical MoaC-family enzyme in Moco biosynthesis; this aligns with literature defining MoaC as the enzyme acting after MoaA in cPMP formation (leimkuhler2016bacterialmolybdoenzymesold pages 2-4, yokoyama2021resolvingthemultidecadelong pages 1-2). | Functional annotation + pathway review | Pseudomonas putida KT2440 protein inferred from conserved bacterial MoaC family | Leimkühler & Iobbi-Nivol 2016 FEMS Microbiol Rev; Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1093/femsre/fuv043 ; https://doi.org/10.1021/acsbiomedchemau.1c00046 | (leimkuhler2016bacterialmolybdoenzymesold pages 2-4, yokoyama2021resolvingthemultidecadelong pages 1-2) |
| Core reaction catalyzed by MoaC | MoaC catalyzes conversion of 3′,8-cH2GTP (the MoaA product) into cyclic pyranopterin monophosphate (cPMP) via a complex rearrangement; thus MoaC is the cPMP synthase and the physiological substrate is 3′,8-cH2GTP, not GTP directly (yokoyama2021resolvingthemultidecadelong pages 4-5, yokoyama2021resolvingthemultidecadelong pages 7-9, yokoyama2018radicalbreakthroughsin pages 4-6, hover2013identificationofa pages 1-2). | Biochemical + mechanistic | Bacterial MoaC; human homolog MOCS1B also tested | Hover et al. 2013 JACS; Yokoyama 2018 Biochemistry; Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1021/ja401781t ; https://doi.org/10.1021/acs.biochem.7b00878 ; https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 4-5, yokoyama2021resolvingthemultidecadelong pages 7-9, yokoyama2018radicalbreakthroughsin pages 4-6, hover2013identificationofa pages 1-2) |
| Pathway placement | cPMP formation is the first committed/conserved step of Moco biosynthesis: GTP is converted by MoaA + MoaC to cPMP, followed by sulfur insertion to MPT and Mo insertion to Moco (yokoyama2021resolvingthemultidecadelong pages 1-2, leimkuhler2016bacterialmolybdoenzymesold pages 1-2, yokoyama2018radicalbreakthroughsin pages 3-4). | Pathway review | Bacteria broadly | Leimkühler & Iobbi-Nivol 2016 FEMS Microbiol Rev; Yokoyama 2018 Biochemistry; Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1093/femsre/fuv043 ; https://doi.org/10.1021/acs.biochem.7b00878 ; https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 1-2, leimkuhler2016bacterialmolybdoenzymesold pages 1-2, yokoyama2018radicalbreakthroughsin pages 3-4) |
| Substrate specificity | Purified 3′,8-cH2GTP is specifically recognized by bacterial MoaC and human MOCS1B; reported Km values are <0.060–0.25 µM for bacterial MoaC and 0.79 µM for human MOCS1B, supporting tight substrate recognition (yokoyama2021resolvingthemultidecadelong pages 4-5, hover2013identificationofa pages 1-2). | Enzyme kinetics | E. coli, S. aureus, human MOCS1B | Hover et al. 2013 JACS; Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1021/ja401781t ; https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 4-5, hover2013identificationofa pages 1-2) |
| Quantitative catalytic parameters | One reported kinetic set for MoaC: Km < 60 nM and kcat = 0.17 min⁻1 for conversion of 3′,8-cH2GTP to cPMP; for comparison, MoaA kcat = 0.043 min⁻1 in the upstream step (yokoyama2018radicalbreakthroughsin pages 4-6). | Enzyme kinetics | Bacterial MoaC / MoaA systems | Yokoyama 2018 Biochemistry | https://doi.org/10.1021/acs.biochem.7b00878 | (yokoyama2018radicalbreakthroughsin pages 4-6) |
| Oligomerization | MoaC forms a hexamer composed of a trimer of dimers; the active site lies at the interface of each dimer, consistent with structural and mutational analyses (yokoyama2021resolvingthemultidecadelong pages 7-9). | Structural biology | Bacterial MoaC | Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 7-9) |
| Active-site pocket | Crystal structures of E. coli MoaC with 3′,8-cH2GTP or cPMP show both ligands occupying the same proposed ligand-binding pocket and contacting the same residue set; these residues are required for in vitro/in vivo function, supporting this pocket as the active site (yokoyama2021resolvingthemultidecadelong pages 4-5). | Structural + mutational | E. coli MoaC | Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 4-5) |
| Conformational dynamics | Two major MoaC conformations were observed: a closed WT form in which K51 in loop 3 interacts with D128, and an open K51A mutant form where loop 3 is dissociated from the active site; loop motion is therefore central to catalysis (yokoyama2021resolvingthemultidecadelong pages 7-9, yokoyama2018radicalbreakthroughsin pages 6-8). | Structural + mechanistic | Bacterial MoaC | Yokoyama 2018 Biochemistry; Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1021/acs.biochem.7b00878 ; https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 7-9, yokoyama2018radicalbreakthroughsin pages 6-8) |
| Mechanistic intermediate X | Active-site variants such as K51A and K131A accumulate an on-pathway intermediate X, described as an acid-labile triaminopyrimidinone nucleoside triphosphate with UV λmax 270 nm and mass 18 Da greater than 3′,8-cH2GTP (yokoyama2018radicalbreakthroughsin pages 6-8). | Mechanistic biochemistry | Bacterial MoaC mutants | Yokoyama 2018 Biochemistry | https://doi.org/10.1021/acs.biochem.7b00878 | (yokoyama2018radicalbreakthroughsin pages 6-8) |
| Inhibitor/trapped intermediate evidence | A noncleavable analog, 3′,8-cH2GMP[CH2]PP, causes irreversible inhibition of MoaC and yields tightly bound compound Y, covalently linked to MoaC and 18 Da smaller than the analog; this supports a multistep rearrangement and covalent/activated intermediate chemistry (yokoyama2018radicalbreakthroughsin pages 6-8, yokoyama2018radicalbreakthroughsin pages 8-9). | Mechanistic biochemistry | Bacterial MoaC | Yokoyama 2018 Biochemistry | https://doi.org/10.1021/acs.biochem.7b00878 | (yokoyama2018radicalbreakthroughsin pages 6-8, yokoyama2018radicalbreakthroughsin pages 8-9) |
| Proposed catalytic residues/mechanism | Mechanistic model assigns roles to D128 (general base in retro-aldol cleavage) and K51/K131 (general acid/base roles in ring expansion/rearrangement); loop closure helps reposition triphosphate for cyclic phosphate formation, and pyranopterin plus cyclic phosphate formation are likely coupled (yokoyama2018radicalbreakthroughsin pages 8-9). | Mechanistic model from structural/biochemical data | Bacterial MoaC | Yokoyama 2018 Biochemistry | https://doi.org/10.1021/acs.biochem.7b00878 | (yokoyama2018radicalbreakthroughsin pages 8-9) |
| Localization inference | No direct P. putida KT2440 localization experiment was found, but bacterial MoaC is treated in the literature as a soluble intracellular/cytosolic biosynthetic enzyme functioning in early Moco biosynthesis rather than a membrane or secreted protein; explicit bacterial localization data were not reported in the extracted passages (yokoyama2021resolvingthemultidecadelong pages 4-5, yokoyama2021resolvingthemultidecadelong pages 7-9, leimkuhler2016bacterialmolybdoenzymesold pages 2-4). | Inference from pathway/biochemistry | Bacteria broadly; inference for P. putida KT2440 | Leimkühler & Iobbi-Nivol 2016 FEMS Microbiol Rev; Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1093/femsre/fuv043 ; https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 4-5, yokoyama2021resolvingthemultidecadelong pages 7-9, leimkuhler2016bacterialmolybdoenzymesold pages 2-4) |
| Pseudomonas interaction-network note | The 2021 perspective notes reported in vivo interactions among MoaA, MoaC, MPT synthase, and sulfur-trafficking enzymes in Pseudomonas aeruginosa based on GFP-PFCA, suggesting MoaC may participate in a broader intracellular Moco-biosynthesis interaction network (yokoyama2021resolvingthemultidecadelong pages 4-5). | Interaction/protein-network evidence | P. aeruginosa | Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1021/acsbiomedchemau.1c00046 | (yokoyama2021resolvingthemultidecadelong pages 4-5) |
| Pseudomonas regulatory note (moaA) | In Pseudomonas spp., regulation of moaA is notable: the moaA 5′ leader contains two CsrA-binding sites and constitutes a MOCO-sensing riboswitch, described as the first riboswitch aptamer known to interact with both a small-molecule ligand and an RNA-binding protein; this is relevant pathway context for MoaC because MoaA and MoaC act together in cPMP synthesis (seyll2013theribonucleoproteincsr pages 6-8). | Regulatory | Pseudomonas context discussed in Csr/Rsm review | Seyll & Van Melderen 2013 Int J Mol Sci | https://doi.org/10.3390/ijms141122117 | (seyll2013theribonucleoproteincsr pages 6-8) |
| KT2440-specific expression evidence | A study of water stress transcriptome dynamics in P. putida KT2440 is cited in the literature extracted here, but the retrieved pages did not provide direct moaC/PP_1292-specific expression values; thus no reliable fold-change for moaC in KT2440 could be extracted from the available context (narihiro2016culturaltranscriptomicand pages 9-10). | Evidence gap / transcriptomic context | P. putida KT2440 | Narihiro et al. 2016 cites Gülez et al. 2012 Appl Environ Microbiol | https://doi.org/10.1128/AEM.06621-11 (cited within retrieved text) | (narihiro2016culturaltranscriptomicand pages 9-10) |
| KT2440-specific annotation limitation | No primary literature in the retrieved set directly characterized PP_1292/moaC in P. putida KT2440 by genetics, phenotype, or localization; therefore functional annotation for Q88NC0 is currently supported mainly by strong family/pathway conservation rather than KT2440-specific wet-lab evidence (leimkuhler2016bacterialmolybdoenzymesold pages 2-4, yokoyama2021resolvingthemultidecadelong pages 1-2). | Evidence synthesis/limitation | P. putida KT2440 | Leimkühler & Iobbi-Nivol 2016 FEMS Microbiol Rev; Yokoyama et al. 2021 ACS Bio Med Chem Au | https://doi.org/10.1093/femsre/fuv043 ; https://doi.org/10.1021/acsbiomedchemau.1c00046 | (leimkuhler2016bacterialmolybdoenzymesold pages 2-4, yokoyama2021resolvingthemultidecadelong pages 1-2) |
Table: This table compiles the most relevant functional, mechanistic, kinetic, and Pseudomonas-specific evidence for MoaC/cPMP synthase, emphasizing what is directly supported by biochemical and structural studies versus what remains inferred for Pseudomonas putida KT2440.
Protein: MoaC (cyclic pyranopterin monophosphate synthase; EC 4.6.1.17)
Molecular function: Catalyzes complex rearrangement of 3′,8-cH2GTP (produced by MoaA) into cyclic pyranopterin monophosphate (cPMP), the first stable committed intermediate of molybdenum cofactor biosynthesis. (yokoyama2021resolvingthemultidecadelong pages 4-5, hover2013identificationofa pages 1-2)
Biological process: Molybdenum cofactor biosynthetic process (early step; cPMP formation upstream of MPT and Mo insertion). (yokoyama2021resolvingthemultidecadelong pages 1-2)
Cellular component (best-available): Cytosolic/intracellular enzyme (inferred from soluble enzyme biochemistry and pathway context; KT2440-specific localization not available). (yokoyama2021resolvingthemultidecadelong pages 7-9, leimkuhler2016bacterialmolybdoenzymesold pages 2-4)
Pathway context: Functions with MoaA; MoaA produces 3′,8-cH2GTP from GTP, and MoaC converts it to cPMP. (yokoyama2021resolvingthemultidecadelong pages 2-3, yokoyama2021resolvingthemultidecadelong pages 7-9)
Key cited sources retrieved and used here include:
References
(leimkuhler2016bacterialmolybdoenzymesold pages 2-4): Silke Leimkühler and Chantal Iobbi-Nivol. Bacterial molybdoenzymes: old enzymes for new purposes. FEMS microbiology reviews, 40 1:1-18, Oct 2016. URL: https://doi.org/10.1093/femsre/fuv043, doi:10.1093/femsre/fuv043. This article has 161 citations and is from a domain leading peer-reviewed journal.
(yokoyama2021resolvingthemultidecadelong pages 1-2): Kenichi Yokoyama, Di Li, and Haoran Pang. Resolving the multidecade-long mystery in moaa radical sam enzyme reveals new opportunities to tackle human health problems. ACS Bio & Med Chem Au, 2:94-108, Dec 2021. URL: https://doi.org/10.1021/acsbiomedchemau.1c00046, doi:10.1021/acsbiomedchemau.1c00046. This article has 8 citations.
(mendel2024thefinalstep pages 1-2): Ralf R. Mendel and Kevin D. Oliphant. The final step in molybdenum cofactor biosynthesis—a historical view. Molecules, 29:4458, Sep 2024. URL: https://doi.org/10.3390/molecules29184458, doi:10.3390/molecules29184458. This article has 8 citations.
(mendel2024thefinalstep pages 2-4): Ralf R. Mendel and Kevin D. Oliphant. The final step in molybdenum cofactor biosynthesis—a historical view. Molecules, 29:4458, Sep 2024. URL: https://doi.org/10.3390/molecules29184458, doi:10.3390/molecules29184458. This article has 8 citations.
(yokoyama2018radicalbreakthroughsin pages 3-4): Kenichi Yokoyama. Radical breakthroughs in natural product and cofactor biosynthesis. Biochemistry, 57 4:390-402, Nov 2018. URL: https://doi.org/10.1021/acs.biochem.7b00878, doi:10.1021/acs.biochem.7b00878. This article has 7 citations and is from a peer-reviewed journal.
(yokoyama2021resolvingthemultidecadelong pages 2-3): Kenichi Yokoyama, Di Li, and Haoran Pang. Resolving the multidecade-long mystery in moaa radical sam enzyme reveals new opportunities to tackle human health problems. ACS Bio & Med Chem Au, 2:94-108, Dec 2021. URL: https://doi.org/10.1021/acsbiomedchemau.1c00046, doi:10.1021/acsbiomedchemau.1c00046. This article has 8 citations.
(yokoyama2021resolvingthemultidecadelong pages 4-5): Kenichi Yokoyama, Di Li, and Haoran Pang. Resolving the multidecade-long mystery in moaa radical sam enzyme reveals new opportunities to tackle human health problems. ACS Bio & Med Chem Au, 2:94-108, Dec 2021. URL: https://doi.org/10.1021/acsbiomedchemau.1c00046, doi:10.1021/acsbiomedchemau.1c00046. This article has 8 citations.
(yokoyama2021resolvingthemultidecadelong pages 7-9): Kenichi Yokoyama, Di Li, and Haoran Pang. Resolving the multidecade-long mystery in moaa radical sam enzyme reveals new opportunities to tackle human health problems. ACS Bio & Med Chem Au, 2:94-108, Dec 2021. URL: https://doi.org/10.1021/acsbiomedchemau.1c00046, doi:10.1021/acsbiomedchemau.1c00046. This article has 8 citations.
(hover2013identificationofa pages 1-2): Bradley M. Hover, Anna Loksztejn, Anthony A. Ribeiro, and Kenichi Yokoyama. Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis. Journal of the American Chemical Society, 135 18:7019-32, May 2013. URL: https://doi.org/10.1021/ja401781t, doi:10.1021/ja401781t. This article has 107 citations and is from a highest quality peer-reviewed journal.
(yokoyama2018radicalbreakthroughsin pages 4-6): Kenichi Yokoyama. Radical breakthroughs in natural product and cofactor biosynthesis. Biochemistry, 57 4:390-402, Nov 2018. URL: https://doi.org/10.1021/acs.biochem.7b00878, doi:10.1021/acs.biochem.7b00878. This article has 7 citations and is from a peer-reviewed journal.
(yokoyama2018radicalbreakthroughsin pages 6-8): Kenichi Yokoyama. Radical breakthroughs in natural product and cofactor biosynthesis. Biochemistry, 57 4:390-402, Nov 2018. URL: https://doi.org/10.1021/acs.biochem.7b00878, doi:10.1021/acs.biochem.7b00878. This article has 7 citations and is from a peer-reviewed journal.
(yokoyama2018radicalbreakthroughsin pages 8-9): Kenichi Yokoyama. Radical breakthroughs in natural product and cofactor biosynthesis. Biochemistry, 57 4:390-402, Nov 2018. URL: https://doi.org/10.1021/acs.biochem.7b00878, doi:10.1021/acs.biochem.7b00878. This article has 7 citations and is from a peer-reviewed journal.
(leimkuhler2016bacterialmolybdoenzymesold pages 1-2): Silke Leimkühler and Chantal Iobbi-Nivol. Bacterial molybdoenzymes: old enzymes for new purposes. FEMS microbiology reviews, 40 1:1-18, Oct 2016. URL: https://doi.org/10.1093/femsre/fuv043, doi:10.1093/femsre/fuv043. This article has 161 citations and is from a domain leading peer-reviewed journal.
(seyll2013theribonucleoproteincsr pages 6-8): Ethel Seyll and Laurence Van Melderen. The ribonucleoprotein csr network. International Journal of Molecular Sciences, 14:22117-22131, Nov 2013. URL: https://doi.org/10.3390/ijms141122117, doi:10.3390/ijms141122117. This article has 24 citations.
(narihiro2016culturaltranscriptomicand pages 9-10): Takashi Narihiro, Yuji Kanosue, and Akira Hiraishi. Cultural, transcriptomic, and proteomic analyses of water-stressed cells of actinobacterial strains isolated from compost: ecological implications in the fed-batch composting process. Microbes and Environments, 31:127-136, May 2016. URL: https://doi.org/10.1264/jsme2.me15199, doi:10.1264/jsme2.me15199. This article has 5 citations and is from a peer-reviewed journal.