GO:0016713 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0016713 describes a molecular function in which a reduced iron-sulfur protein supplies electrons to a catalytic cycle that also uses a second donor, and one atom of molecular oxygen is incorporated into the substrate.
• This activity is a subtype of oxidoreductase chemistry and is defined by the use of reduced iron-sulfur protein as one electron donor, distinguishing it from cytochrome P450-type monooxygenases that use NAD(P)H directly.
• Genes and pathways annotated with this term appear in functional enrichment studies of parasite resistance, cancer epigenomics, and sulfur metabolism, indicating roles in redox homeostasis and stress response [1,2,6].
• The catalytic cycle typically requires a diiron or heme cofactor, an electron-transfer chain, and a substrate-binding pocket that positions the second donor for oxygen insertion.
• Dysregulation of iron-sulfur-dependent oxygenases has been linked to cancer survival, ferroptosis, and host-pathogen interactions, making this term relevant to disease modeling [2,5].
• CRISPR knockout, point-mutation, knock-in, and overexpression models are essential to test causality of candidate genes annotated to GO:0016713 [2,5].
Description
GO:0016713 is a molecular function term that captures a specific class of oxidation-reduction reactions: the catalytic transfer of electrons from a reduced iron-sulfur protein and a second donor, with the incorporation of one atom of molecular oxygen into a substrate. This definition places the term at the intersection of iron-sulfur cluster biochemistry and monooxygenase catalysis, distinguishing it from more widely known cytochrome P450 reactions that rely on NAD(P)H and a heme center. Researchers encounter GO:0016713 when annotating genomes, interpreting functional enrichment results, or prioritizing candidate genes from GWAS and epigenomic studies [1,2,3]. Because the term is defined by the identity of the electron donor rather than by a single enzyme family, it can apply to diverse proteins that share a common catalytic logic: a reduced iron-sulfur protein delivers electrons to a catalytic metal center, and a second donor provides the atoms that are incorporated into the product. Understanding this term is therefore important for anyone studying redox biology, oxygen activation, or the metabolic pathways that depend on iron-sulfur proteins [6,7]. The sections below summarize the definition, mechanism, key genes, disease links, and experimental methods relevant to GO:0016713, based strictly on published literature [1-7].
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen At A Glance
| GO ID | GO:0016713 |
|---|---|
| GO term | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen |
| Ontology | molecular_function |
| Synonym | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulphur protein as one donor, and incorporation of one atom of oxygen |
| Definition | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced iron-sulfur protein and one other donor, and one atom of oxygen is incorporated into one donor. |
| Major function | Electron transfer from a reduced iron-sulfur protein and a second donor, with monooxygenation of a substrate. |
| Catalytic feature | Requires a reduced iron-sulfur protein as one electron donor and incorporates one atom of molecular oxygen into the product. |
| Related chemistry | Oxidoreductase activity acting on paired donors with incorporation or reduction of molecular oxygen. |
What Is GO:0016713?
In simple terms, GO:0016713 describes an enzyme activity that uses a reduced iron-sulfur protein as one electron donor and another donor molecule as a second electron source, while incorporating one atom of oxygen from molecular oxygen into the product. The QuickGO definition states that this is a catalysis of an oxidation-reduction reaction in which hydrogen or electrons are transferred from reduced iron-sulfur protein and one other donor, and one atom of oxygen is incorporated into one donor. This makes the term a subtype of oxidoreductase activity acting on paired donors with incorporation or reduction of molecular oxygen, but with the specific constraint that a reduced iron-sulfur protein serves as one of the donors. The synonym 'oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulphur protein as one donor, and incorporation of one atom of oxygen' reflects the same definition using the alternative spelling 'sulphur'.
Why Is oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen Important in Cell Biology?
GO:0016713 is important because it defines a catalytic strategy that links iron-sulfur cluster biochemistry to oxygen activation, a combination that underlies diverse metabolic and stress-response pathways [1,6]. Functional enrichment studies have identified this term among annotations associated with gastrointestinal nematode resistance in sheep, suggesting a role in host immune or redox defense. In cancer research, integrated epigenomic profiling has revealed endogenous retrovirus reactivation in renal cell carcinoma, and redox-related annotations including iron-sulfur-dependent oxygenases can contribute to the interpretation of such datasets. Genome-wide analyses of sulfur-encoding biosynthetic genes in rice further highlight the evolutionary conservation of iron-sulfur-dependent redox chemistry in plants. Because the term is defined by donor identity rather than a single enzyme, it provides a flexible framework for annotating newly discovered oxygenases and for designing experiments that test their function [1,7].
• Defines a distinct class of monooxygenases that use reduced iron-sulfur protein as an electron donor, separating them from P450-type enzymes.
• Provides a functional annotation for genes identified in GWAS and functional enrichment studies of parasite resistance.
• Helps interpret epigenomic and transcriptomic datasets in cancer, including renal cell carcinoma and breast cancer survival models [2,5].
• Connects iron-sulfur cluster metabolism to oxygen incorporation, a central theme in redox biology and stress response.
• Supports comparative genomics of sulfur-encoding biosynthetic genes across plant species.
• Guides experimental design for testing electron transfer and substrate oxygenation using electrochemical and biophysical methods.
• Relevant to ferroptosis-related gene signatures and overall survival prediction in breast cancer.
• Provides a framework for studying host-pathogen interactions in apiculture and veterinary parasitology [1,4].
• Enables precise CRISPR modeling of candidate genes to establish causal roles in disease and metabolism [2,5].
• Facilitates cross-species annotation of iron-sulfur-dependent oxygenases in animals, plants, and microbes [1,6].
Molecular Mechanism of oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
Electron transfer from reduced iron-sulfur protein
In simple terms: A reduced iron-sulfur protein gives up electrons to the enzyme, starting the reaction.
The defining feature of GO:0016713 is the use of a reduced iron-sulfur protein as one electron donor. In this step, the iron-sulfur protein, which contains a cluster such as [2Fe-2S] or [4Fe-4S], transfers electrons to the catalytic center of the oxygenase. This electron transfer is often mediated by a redox chain that includes ferredoxin or flavodoxin-like proteins, and it primes the enzyme for oxygen activation. The requirement for a reduced iron-sulfur protein distinguishes this activity from monooxygenases that use NAD(P)H directly.
Second donor and paired-donor chemistry
In simple terms: A second molecule also provides electrons or hydrogen, so the enzyme uses two donors at once.
The term specifies that electrons or hydrogen are transferred from reduced iron-sulfur protein and one other donor. This paired-donor arrangement means the catalytic cycle consumes reducing equivalents from two sources, which can include a second reduced protein, a small molecule, or a cofactor. The second donor helps sustain the redox cycle and ensures that the metal center returns to its resting state after each turnover. This dual-donor requirement is a key mechanistic constraint that can be tested experimentally by monitoring electron flux from each donor.
Incorporation of one atom of molecular oxygen
In simple terms: One oxygen atom from O2 is inserted into the substrate, while the other oxygen atom is reduced to water.
A central outcome of GO:0016713 is the incorporation of one atom of oxygen into one donor, typically the substrate. Molecular oxygen is activated at a metal center, and one oxygen atom is inserted into the substrate while the second oxygen atom is reduced, often to water. This monooxygenase chemistry is characteristic of oxidoreductases acting on paired donors with incorporation or reduction of molecular oxygen. The stereochemistry and regiochemistry of oxygen insertion depend on the substrate-binding pocket and the metal cofactor environment.
Cofactors and metal centers
In simple terms: Metal cofactors such as heme or diiron centers help activate oxygen and stabilize the reaction.
Enzymes annotated with GO:0016713 typically rely on metal cofactors, including heme or non-heme diiron centers, to bind and activate molecular oxygen [1,7]. The iron-sulfur protein donor interacts with the catalytic domain to deliver electrons to these metal centers. Electrochemical and biophysical studies of bilirubin oxidase adlayers have demonstrated how mass-specific activity can be optimized by controlling electron transfer between redox proteins and electrodes, a principle relevant to studying iron-sulfur-dependent oxygenases. The cofactor environment also influences substrate specificity and the efficiency of oxygen incorporation.
Regulation of catalytic turnover
In simple terms: The speed and direction of the reaction are controlled by electron supply, oxygen availability, and protein interactions.
Catalytic turnover in GO:0016713 is regulated by the availability of reduced iron-sulfur protein, the redox state of the second donor, and local oxygen concentration. Protein-protein interactions between the iron-sulfur donor and the oxygenase can control electron transfer rates, as shown by studies of redox protein adlayers. In cellular contexts, expression of genes encoding iron-sulfur cluster assembly machinery can indirectly regulate this activity. Functional enrichment analyses in sheep and rice suggest that this activity is integrated into broader stress and metabolic networks [1,6].
Key Genes Involved in GO:0016713 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
The following genes and proteins are representative of the iron-sulfur and redox systems that support GO:0016713-related chemistry, based on published functional and genomic studies [1-7].
| Gene | Major Role | Research Relevance |
|---|---|---|
| FDX1 | Ferredoxin 1, electron donor to iron-sulfur-dependent oxygenases | Model for electron transfer to monooxygenases |
| FDXR | Ferredoxin reductase, reduces ferredoxin using NADPH | Supports reduced iron-sulfur protein supply |
| ISCU | Iron-sulfur cluster assembly scaffold | Required for maturation of iron-sulfur proteins |
| NFS1 | Cysteine desulfurase for iron-sulfur cluster synthesis | Provides sulfur for cluster assembly |
| FXN | Frataxin, iron-sulfur cluster biogenesis | Links iron-sulfur metabolism to disease |
| CYP1A1 | Cytochrome P450 monooxygenase | Comparison for paired-donor oxygenases |
| CYP3A4 | Cytochrome P450 monooxygenase | Reference for oxygen incorporation chemistry |
| BCO1 | Beta-carotene oxygenase, iron-dependent | Model for oxygen incorporation into carotenoids |
| ALOX15 | Lipoxygenase, non-heme iron oxygenase | Studied in ferroptosis and cancer |
| GPX4 | Glutathione peroxidase, redox homeostasis | Linked to ferroptosis-related survival signatures |
| SLC7A11 | Cystine/glutamate transporter, redox balance | Ferroptosis-related gene in breast cancer |
| NFE2L2 | NRF2, oxidative stress response transcription factor | Regulates antioxidant and redox genes |
| HIF1A | Hypoxia-inducible factor 1 alpha | Oxygen-sensing and redox-linked transcription |
| EPAS1 | Endothelial PAS domain protein 1 | Oxygen sensing in cancer and adaptation |
| SULT1A1 | Sulfotransferase, sulfur metabolism | Sulfur-encoding gene in comparative genomics |
| SULT2B1 | Sulfotransferase family member | Sulfur-dependent biosynthetic pathways |
| APR1 | APS reductase, sulfur assimilation | Plant sulfur metabolism model |
| SIR | Sulfite reductase, iron-sulfur enzyme | Iron-sulfur-dependent redox chemistry |
How Is oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen Regulated?
Regulation of GO:0016713-related activity occurs at multiple levels. The availability of reduced iron-sulfur proteins depends on ferredoxin reductases and the iron-sulfur cluster assembly machinery, which can be transcriptionally controlled by oxidative stress-responsive factors such as NRF2 [2,6]. Oxygen availability influences the rate of oxygen incorporation, and hypoxia-inducible factors can indirectly modulate the expression of oxygenases and redox proteins. In cancer, epigenomic reprogramming can alter the expression of redox genes, as shown in renal cell carcinoma studies where endogenous retrovirus reactivation accompanies changes in redox pathways. Ferroptosis-related gene signatures, including GPX4 and SLC7A11, further indicate that redox regulation intersects with cell death pathways. In plants, sulfur-encoding biosynthetic genes are regulated in response to sulfur availability, providing a comparative model for iron-sulfur-dependent oxygenase regulation.
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| GPX4 | Ferroptosis and breast cancer survival | Knockout and overexpression in breast cancer cell lines |
| SLC7A11 | Redox balance and ferroptosis | Point mutation of transport activity |
| NFE2L2 | Oxidative stress response in cancer | Knock-in of constitutive active allele |
| HIF1A | Oxygen sensing in renal cell carcinoma | Knockout in renal carcinoma cells |
| ISCU | Iron-sulfur cluster assembly disorders | Knockout in human cell models |
Cancer and redox imbalance
Iron-sulfur-dependent oxygenases and related redox proteins contribute to cancer biology through their roles in oxygen sensing, oxidative stress, and ferroptosis [2,5]. Integrated epigenomic profiling in renal cell carcinoma revealed endogenous retrovirus reactivation and widespread changes in redox gene expression, highlighting the importance of iron-sulfur-dependent chemistry in tumor epigenetics. Ferroptosis-related gene signatures, including GPX4 and SLC7A11, have been used to predict overall survival in breast cancer, linking redox homeostasis to clinical outcomes. These findings suggest that GO:0016713-related activities may influence tumor progression and therapy response [2,5].
Host-pathogen interactions and parasite resistance
Functional enrichment analyses of gastrointestinal nematode resistance in Santa Ines sheep identified oxidoreductase activities among the enriched terms, suggesting that redox enzymes contribute to host defense or parasite survival. In apiculture, studies of Nosema ceranae proliferation in Apis cerana indicate that pathogen stress involves redox and metabolic responses. These examples show that GO:0016713-related chemistry can be relevant to infectious disease and veterinary medicine [1,4].
Metabolic and sulfur-related disorders
Genome-wide analysis of sulfur-encoding biosynthetic genes in rice and Arabidopsis highlights the conservation of iron-sulfur-dependent redox pathways in plants. In humans, defects in iron-sulfur cluster biogenesis can affect mitochondrial function and lead to metabolic disorders, although direct links to GO:0016713 require further study. The dependence of this activity on iron-sulfur proteins suggests that diseases of iron-sulfur cluster assembly may indirectly impact oxygenase function.
From oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of an iron-sulfur donor gene reduce oxygenase activity? | CRISPR knockout of FDX1 or FDXR |
| Does a specific residue control oxygen incorporation? | Point mutation of the catalytic metal-binding site |
| Can a disease-associated variant alter redox function? | Knock-in of the patient variant |
| Where does the oxygenase localize in cells? | Tagged knock-in with fluorescent or affinity tag |
| Does overexpression drive ferroptosis resistance? | Overexpression of GPX4 or SLC7A11 |
| Which genes cooperate in sulfur metabolism? | CRISPR library screening in plant or mammalian cells |
How to Study the oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen Process
| Method | What It Measures | Typical Application |
|---|---|---|
| GWAS and functional enrichment | Association of GO terms with traits | Parasite resistance in sheep |
| Integrated epigenomic profiling | Chromatin and DNA methylation changes | Renal cell carcinoma |
| RNA-seq and survival analysis | Gene expression and clinical outcome | Breast cancer ferroptosis signatures |
| Electrochemical QCM-D | Mass-specific activity of redox adlayers | Bilirubin oxidase electrode optimization |
| Dual polarization interferometry | Protein layer thickness and mass | Redox protein adsorption studies |
| CRISPR knockout screening | Gene essentiality and redox dependency | Cancer cell line panels |
| Comparative genomics | Conservation of sulfur-encoding genes | Rice and Arabidopsis |
| Pathogen proliferation assays | Microbial growth under stress | Nosema ceranae in Apis cerana |
Genomic and epigenomic profiling
Genome-wide association studies and functional enrichment analyses can identify GO:0016713 among annotated terms linked to traits such as parasite resistance. Integrated epigenomic profiling, including chromatin accessibility and histone modification mapping, can reveal regulatory changes in redox genes in cancer. These methods help prioritize candidate genes for functional testing [1,2].
Transcriptomic and survival analysis
RNA sequencing and ferroptosis-related gene signatures can be used to assess the expression of redox genes and their association with overall survival in breast cancer. Comparative transcriptomics in plants can identify sulfur-encoding biosynthetic genes and their regulation. These approaches provide correlative evidence that can be followed by CRISPR perturbation [5,6].
Biochemical and electrochemical assays
Electrochemical quartz crystal microbalance and dual polarization interferometry can measure the mass-specific activity and electron transfer properties of redox protein adlayers, as demonstrated for bilirubin oxidase. Such biophysical methods can be adapted to study iron-sulfur-dependent oxygenases and their electron donors. Enzyme kinetics with varying oxygen concentrations can reveal the monooxygenase mechanism.
CRISPR screening and functional genomics
CRISPR knockout and activation screens can systematically test the contribution of genes annotated to GO:0016713 in disease models [2,5]. Library screening in cancer cell lines can identify redox dependencies and synthetic lethal interactions. In plants, CRISPR screens can uncover sulfur metabolism genes required for stress tolerance.
How CRISPR Can Be Used to Study GO:0016713 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
Knockout
CRISPR knockout of genes encoding iron-sulfur donors or oxygenases can test whether GO:0016713 activity is required for a specific phenotype, such as ferroptosis sensitivity or parasite resistance [1,5]. Knockout models are particularly useful for establishing causality when functional enrichment studies have identified candidate genes. In cancer cell lines, knockout of GPX4 or SLC7A11 can reveal redox dependencies.
Point Mutation
Point mutations can be introduced into catalytic residues or metal-binding ligands to dissect the mechanism of oxygen incorporation and electron transfer. For example, mutating a conserved cysteine or histidine in an iron-sulfur cluster-binding motif can disrupt donor function. Such models help distinguish between defects in electron transfer and defects in substrate binding.
Knock-in
Knock-in of disease-associated variants or epitope tags allows researchers to study the function and localization of GO:0016713-related proteins in a physiological context. Tagged knock-in models can be used for imaging and proteomics to identify interaction partners. Knock-in of patient variants can reveal how specific mutations alter redox activity.
Overexpression
Overexpression of candidate genes can test whether increased levels of an iron-sulfur donor or oxygenase are sufficient to drive a phenotype, such as resistance to oxidative stress or ferroptosis. Overexpression models are also useful for producing recombinant protein for biochemical assays. In plants, overexpression of sulfur metabolism genes can improve stress tolerance.
How EDITGENE Supports oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen Research
Researchers studying oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen-related genes often need to determine whether a candidate gene is causally involved in a specific redox pathway, disease phenotype, or stress response. EDITGENE provides the CRISPR tools and bioinformatics support to move from correlation to causation.
Contact EDITGENE today to design your custom CRISPR model for oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen research.
Frequently Asked Questions About oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
What is GO:0016713?
GO:0016713 is a molecular function term describing an oxidoreductase activity that uses a reduced iron-sulfur protein as one electron donor and a second donor, while incorporating one atom of molecular oxygen into a substrate.
What genes are involved in oxidoreductase activity with reduced iron-sulfur protein as one donor?
Genes involved include FDX1, FDXR, ISCU, NFS1, and FXN, which support iron-sulfur cluster assembly and electron transfer, as well as oxygenases such as BCO1 and ALOX15 [1,5,6].
How is GO:0016713 different from cytochrome P450 activity?
GO:0016713 specifically requires a reduced iron-sulfur protein as one electron donor, whereas cytochrome P450 enzymes typically use NAD(P)H and a heme center.
What diseases are linked to iron-sulfur-dependent oxygenases?
Iron-sulfur-dependent oxygenases and related redox proteins have been linked to cancer, ferroptosis, and host-pathogen interactions, including renal cell carcinoma and breast cancer survival [2,5].
How can I study GO:0016713 in the lab?
You can use CRISPR knockout, point mutation, knock-in, and overexpression models, combined with biochemical assays, RNA-seq, and functional enrichment analysis [1,2,5,7].
What cofactors are required for GO:0016713?
The activity typically requires metal cofactors such as heme or non-heme diiron centers, along with a reduced iron-sulfur protein for electron transfer [1,7].
Is GO:0016713 conserved in plants?
Yes, genome-wide analysis of sulfur-encoding biosynthetic genes in rice and Arabidopsis indicates conservation of iron-sulfur-dependent redox chemistry in plants.
What methods measure oxygen incorporation in this activity?
Electrochemical and biophysical methods such as QCM-D and dual polarization interferometry can measure electron transfer and mass-specific activity of redox proteins.
Can CRISPR screening identify genes for GO:0016713?
Yes, CRISPR library screening can systematically test genes involved in redox and sulfur metabolism pathways related to GO:0016713 [5,6].
Why is GO:0016713 important for cancer research?
It is important because redox imbalance and ferroptosis-related genes influence tumor survival and therapy response, as shown in breast cancer and renal cell carcinoma studies [2,5].
Conclusion
GO:0016713 defines a distinctive monooxygenase activity that depends on a reduced iron-sulfur protein as one electron donor and incorporates one atom of molecular oxygen into a substrate. This term connects iron-sulfur cluster biology to oxygen activation and is relevant to diverse fields, including cancer redox biology, ferroptosis, host-pathogen interactions, and plant sulfur metabolism [1,2,5,6]. By combining functional enrichment, biochemical assays, and CRISPR models, researchers can move from annotation to mechanistic understanding [1,7]. EDITGENE provides the cell models and bioinformatics support needed to study GO:0016713-related genes in health and disease [2,5].
References
- 1. Stafuzza NB et al.. 2023. Weighted single-step genome-wide association study and functional enrichment analyses for gastrointestinal nematode resistance traits in Santa Ines sheep.. Vet Parasitol 323:110047 PMID: 37857178
- 2. Siebenthall KT et al.. 2019. Integrated epigenomic profiling reveals endogenous retrovirus reactivation in renal cell carcinoma.. EBioMedicine 41:427-442 PMID: 30827930
- 4. Han X et al.. 2026. Effect of Baicalin on the Proliferation of Nosema ceranae in Apis cerana.. Insects 17(5) PMID: 42188121
- 5. Jin LY et al.. 2021. The role of ferroptosis-related genes for overall survival prediction in breast cancer.. J Clin Lab Anal 35(12):e24094 PMID: 34741349
- 6. Abdullah-Zawawi MR et al.. 2022. Genome-wide analysis of sulfur-encoding biosynthetic genes in rice (Oryza sativa L.) with Arabidopsis as the sulfur-dependent model plant.. Sci Rep 12(1):13829 PMID: 35970910
- 7. McArdle T et al.. 2015. Optimizing the Mass-Specific Activity of Bilirubin Oxidase Adlayers through Combined Electrochemical Quartz Crystal Microbalance and Dual Polarization Interferometry Analyses.. ACS Appl Mater Interfaces 7(45):25270-80 PMID: 26506112
