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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 identity check is positive. The literature’s S. pombe cao1⁺, formerly spao1, is ORF SPAC2E1P3.04 and corresponds to the supplied Q9P7F2 record. It encodes the experimentally active copper-dependent primary-amine oxidase Cao1, not the separate predicted paralog Cao2 and not a similarly named gene from another organism. Deleting cao1 eliminates detectable ethylamine-oxidizing activity, whereas deleting cao2 does not, providing a strong functional identity test (peter2008élucidationdunmécanismea pages 59-63, peter2008copperdistributedby pages 2-2, peter2008élucidationdunmécanisme pages 59-63).
Cao1 is best annotated as a predominantly cytosolic copper/topaquinone-dependent primary-amine oxidase that supports nitrogen acquisition from primary amines. Its demonstrated reaction is:
R–CH₂–NH₂ + O₂ + H₂O → R–CHO + NH₃ + H₂O₂.
Ethylamine is the clearest physiologically validated substrate: cao1Δ cells cannot grow when ethylamine is the sole nitrogen source, and reintegration of cao1⁺ restores growth. In biochemical substrate tests, Cao1 oxidized all primary amines examined; ethylamine, putrescine, and 1,8-diaminooctane were the best substrates, while benzylamine was less efficiently oxidized. No reliable Cao1-specific Km, kcat, or catalytic-efficiency values were found (peter2008élucidationdunmécanismea pages 70-73, peter2008élucidationdunmécanisme pages 66-70, peter2008élucidationdunmécanismea pages 66-70).
| Annotation topic | Best-supported conclusion | Evidence type/directness | Key quantitative result | Principal source/date/DOI URL |
|---|---|---|---|---|
| Identity | The target is Schizosaccharomyces pombe cao1⁺/spao1, ORF SPAC2E1P3.04, corresponding to Cao1/Q9P7F2; it is distinct from the separate paralog Cao2 and from similarly named genes in other organisms. Only Cao1 accounts for detectable CAO activity under the tested conditions. | Direct genetic, expression, and enzyme evidence; accession correspondence relies on the supplied UniProt record. | cao1Δ abolished detectable ethylamine-oxidizing activity, whereas cao2Δ retained approximately wild-type activity. | Peter et al., October 2008, Eukaryotic Cell, DOI 10.1128/EC.00230-08 (peter2008copperdistributedby pages 2-2, peter2008élucidationdunmécanisme pages 59-63) |
| Reaction and substrates | Cao1 oxidatively deaminates primary amines: R–CH₂–NH₂ + O₂ + H₂O → R–CHO + NH₃ + H₂O₂. Ethylamine is a directly demonstrated physiological substrate; a tested panel indicates broad primary-amine activity, strongest with ethylamine, putrescine, and 1,8-diaminooctane, with weaker benzylamine oxidation. No reliable Cao1-specific kinetic constants were located. | Reaction demonstrated by enzyme assays; substrate ranking reported experimentally, but detailed kinetics are unavailable. | All tested primary amines were oxidized; no supported Kₘ or kcat values were reported in the retrieved evidence. | Peter et al., October 2008, DOI 10.1128/EC.00230-08; Peter thesis, 2008 (peter2008élucidationdunmécanismea pages 70-73, peter2008copperdistributedby pages 7-8) |
| Cofactors and catalytic residues | Cao1 belongs to the copper/topaquinone oxidase family. Copper dependence is direct; one copper ion and TPQ per active site and copper/O₂-dependent conversion of a Tyr precursor to TPQ are strongly supported at family level. Cao1 residues His458, His460, and His627 are essential for activity and align with the conserved copper-binding catalytic region. | Direct copper-dependence and site-directed mutagenesis; TPQ stoichiometry/biogenesis is principally family-level mechanistic inference rather than direct Cao1 chemical analysis. | H458A, H460A, and H627A: no detectable activity; H456A: about 5.9-fold lower than wild type; H621A: near wild type. | Peter et al., October 2008, DOI 10.1128/EC.00230-08 (peter2008copperdistributedby pages 1-2, peter2008élucidationdunmécanismea pages 59-63) |
| Domains/family alignment | The supplied InterPro assignments—Cu_Am_Ox_Cu-bd, Cu_Am_ox_TPQ-bd, Cu_amine_oxidase, and C-terminal Cu-amine-oxidase domains—agree with the conserved TPQ-precursor and copper-ligating histidines found in Cao1. | Sequence/domain inference corroborated by loss-of-function mutagenesis; no Cao1 experimental structure was located. | Cao1 was reported to share 57% sequence identity with Hansenula polymorpha methylamine oxidase HPAO. | Peter et al., October 2008, DOI 10.1128/EC.00230-08 (peter2008élucidationdunmécanismea pages 59-63, peter2008élucidationdunmécanisme pages 59-63) |
| Cellular localization | A functional Cao1–GFP fusion is distributed predominantly and uniformly in the cytosol and is excluded from the nucleus in vegetative cells. Evidence does not support secretion or membrane residence. | Direct fluorescence microscopy using an activity-retaining fusion protein. | Cao1–GFP retained activity comparable to untagged Cao1; localization was qualitative. | Peter et al., October 2008, DOI 10.1128/EC.00230-08 (peter2008élucidationdunmécanismea pages 59-63, peter2008copperdistributedby pages 7-8) |
| Copper uptake and intracellular delivery | Under copper limitation, extracellular copper reaches Cao1 mainly through Cuf1-regulated high-affinity Ctr4–Ctr5 uptake, followed by intracellular delivery involving Atx1. Copper supplementation bypasses transporter/regulatory defects. Ccc2, Cox17, and Pccs were not required under the tested conditions, implying a residual unidentified delivery route. | Direct deletion, rescue, protein-expression, enzyme-activity, and yeast two-hybrid evidence; direct metal transfer itself was not biochemically visualized. | atx1Δ lowered Cao1 activity by about 70–80%; Cao1–Atx1 interaction was 2.84 Miller units versus about 0.24 for controls and rose to 6.20 with TTM. Approximately 10 µM CuSO₄ restored activity in uptake-defective strains. | Peter et al., October 2008, DOI 10.1128/EC.00230-08 (peter2008élucidationdunmécanisme pages 66-70, peter2008élucidationdunmécanismea pages 63-66, peter2008copperdistributedby pages 12-13) |
| Physiological role and regulation | Cao1 enables assimilation of ethylamine as a sole nitrogen source, linking amine catabolism to nitrogen acquisition. cao1⁺ is induced by nitrogen limitation but is not materially regulated by copper or Cuf1 at the transcript level; copper instead controls enzyme maturation/activity. | Direct growth complementation, transcript, and enzyme evidence. | cao1Δ cells failed to grow on ethylamine as sole nitrogen source; reintegration of cao1⁺ restored growth. | Peter et al., October 2008, DOI 10.1128/EC.00230-08 (peter2008élucidationdunmécanisme pages 66-70, peter2008élucidationdunmécanismea pages 66-70) |
| Meiosis and sporulation | Cao1 activity is maintained through development by temporally coordinated copper transport: early Ctr4–Ctr5 uptake, later Ctr6-mediated mobilization of vacuolar copper, and meiosis-specific Mfc1 delivery to prespores. Comparable Cao1 protein abundance despite reduced activity supports defective copper loading rather than reduced expression. | Direct developmental genetics, immunoblotting, copper rescue, and CAO activity assays; some spatial assignment is pathway interpretation based on transporter localization. | At 9 h of meiosis, deleting mfc1 in a ctr4Δ ctr6Δ background reduced CAO activity by 43% versus the double mutant and 79% versus wild type; copper supplementation restored/increased activity. | Plante et al., April 2014, Journal of Biological Chemistry, DOI 10.1074/jbc.M113.543678 (plante2014characterizationofschizosaccharomyces pages 11-12, plante2014characterizationofschizosaccharomyces pages 13-14) |
| 2023–2024 evidence gap | No target-specific 2023–2024 primary study on Q9P7F2/Cao1 was identified in the retrieved literature. Consequently, the most precise functional annotation still rests mainly on the 2008 mechanistic study and 2014 meiotic copper-transport work; recent findings about unrelated CAO1 symbols or other copper amine oxidases should not be transferred automatically. | Evidence-gap assessment from target-, accession-, ORF-, synonym-, organism-, and family-specific searches; not evidence that no unpublished work exists. | Latest target-specific primary study retrieved: 2014; no Cao1-specific structural model validation, purified-enzyme kinetics, or direct TPQ spectroscopy was found. | Evidence synthesis based on Peter et al., 2008 and Plante et al., 2014 (peter2008copperdistributedby pages 1-2, plante2014characterizationofschizosaccharomyces pages 11-12) |
Table: Evidence-graded annotation of fission-yeast Cao1/Q9P7F2, separating direct experimental findings from family-level inference. It also identifies quantitative results and the absence of target-specific 2023–2024 research in the retrieved literature.
The direct study by Peter et al., published October 2008 in Eukaryotic Cell, identifies SPAC2E1P3.04 as cao1⁺/SpaO1 and shows that expression of this gene produces the active S. pombe amine oxidase. The paper is available at https://doi.org/10.1128/EC.00230-08. Cao1 reportedly shares 57% sequence identity with the Hansenula polymorpha methylamine oxidase HPAO and contains the conserved TPQ-precursor and copper-binding region characteristic of copper amine oxidases (peter2008élucidationdunmécanismea pages 59-63, peter2008copperdistributedby pages 1-2).
The supplied InterPro assignments—Cu_Am_Ox_Cu-bd, Cu_Am_ox_TPQ-bd, Cu_amine_oxidase, and the C-terminal copper-amine-oxidase domains/superfamily—therefore align well with the literature. Importantly, this alignment is supported not only by sequence similarity but also by copper-dependent activity and loss-of-function substitutions in conserved C-terminal histidines (peter2008élucidationdunmécanisme pages 59-63, peter2008élucidationdunmécanismea pages 59-63).
Cao1 catalyzes oxidative deamination of primary amines, producing the corresponding aldehyde, ammonia, and hydrogen peroxide. Activity was assayed with ethylamine using chemiluminescent, spectrophotometric, and peroxidase-coupled methods. A functional Cao1–GFP fusion retained activity comparable to untagged Cao1, supporting the validity of subsequent localization and copper-delivery experiments (peter2008élucidationdunmécanismea pages 66-70, peter2008copperdistributedby pages 7-8).
The available substrate panel indicates broad rather than narrowly monospecific activity. Ethylamine, putrescine, and 1,8-diaminooctane gave the strongest activity among tested substrates; benzylamine was poorer. Thus, the most defensible specificity annotation is broad primary-amine oxidase with experimentally favored small aliphatic monoamines and selected diamines, rather than a strictly ethylamine-specific enzyme. Because the retrieved work did not provide purified-enzyme kinetic constants, the precise in-vivo substrate hierarchy remains incompletely resolved (peter2008élucidationdunmécanismea pages 70-73).
The biological validation is strongest for ethylamine catabolism. Loss of Cao1 prevents growth on ethylamine as sole nitrogen source, while genetic restoration of cao1⁺ rescues growth. Cao1 therefore links amine oxidation directly to nitrogen assimilation, with the released ammonia providing usable nitrogen (peter2008élucidationdunmécanisme pages 66-70, peter2008élucidationdunmécanismea pages 66-70).
Copper dependence is experimentally secure. Under copper limitation, defects in high-affinity uptake or intracellular copper delivery sharply reduce or abolish Cao1 activity despite continued production of Cao1 protein; exogenous copper restores activity. This demonstrates that copper controls enzyme maturation or activation, rather than simply cao1 transcription (peter2008élucidationdunmécanismea pages 63-66, peter2008élucidationdunmécanisme pages 63-66).
Copper/topaquinone oxidases generally contain one copper ion and one covalently generated TPQ cofactor per active site. Copper and molecular oxygen support autocatalytic conversion of a conserved tyrosine precursor into TPQ. For Q9P7F2, the conserved precursor motif and family assignment strongly support this chemistry, but the retrieved evidence did not include direct Cao1-specific TPQ spectroscopy, cofactor stoichiometry, or an experimental three-dimensional structure. TPQ details should therefore be regarded as strong family-based inference integrated with direct copper-dependent function, rather than direct chemical characterization of purified Q9P7F2 (peter2008copperdistributedby pages 1-2, peter2008élucidationdunmécanisme pages 59-63).
Site-directed mutagenesis provides direct active-site evidence. H458A, H460A, and H627A substitutions abolished detectable Cao1 activity. H456A retained only approximately one-sixth of wild-type activity—a 5.9-fold reduction—whereas H621A remained near wild type. These results strongly support His458, His460, and His627 as essential components of the conserved copper-dependent catalytic region, while showing that not every nearby histidine is indispensable (peter2008élucidationdunmécanismea pages 59-63).
In vegetatively growing cells, an activity-retaining Cao1–GFP fusion showed relatively uniform cytosolic fluorescence and was excluded from the DAPI-stained nucleus. Free GFP entered both cytoplasm and nucleus, making the nuclear exclusion meaningful. No evidence in the retrieved studies supports secretion, plasma-membrane anchoring, or residence in an organelle under these conditions (peter2008élucidationdunmécanismea pages 59-63, peter2008élucidationdunmécanisme pages 63-66).
During late meiosis and sporulation, the copper-supply machinery is reorganized around developing prespores. The literature interprets Cao1 activity in this context as requiring copper accumulation within the spore compartment, but the strongest direct localization evidence for Cao1 itself remains the vegetative-cell cytosolic Cao1–GFP experiment. Developmental spatial conclusions partly derive from transporter localization and stage-specific activity measurements and should not be overstated as direct high-resolution Cao1 imaging (plante2014characterizationofschizosaccharomyces pages 11-12, plante2014characterizationofschizosaccharomyces pages 13-14).
Under copper limitation, Cao1 activation depends on the Cuf1-regulated high-affinity Ctr4–Ctr5 copper-import system. Deleting cuf1, or both ctr4 and ctr5, eliminated detectable CAO activity under chelation even though Cao1–GFP was produced. Addition of 10 µM CuSO₄ restored activity, consistent with high extracellular copper bypassing the high-affinity pathway through lower-affinity uptake. Under copper-replete conditions, cuf1Δ and ctr4Δ ctr5Δ strains retained approximately 59% and 45% of wild-type activity, respectively (peter2008élucidationdunmécanismea pages 63-66, peter2008élucidationdunmécanisme pages 63-66).
After uptake, Atx1 supplies most of the copper needed for Cao1 activation. atx1Δ reduced Cao1 activity by approximately 70–80%, or 2.6–3.2-fold relative to relevant controls, without a corresponding loss of Cao1 protein; copper supplementation and re-expression of atx1⁺ substantially rescued activity (peter2008élucidationdunmécanisme pages 66-70, peter2008copperdistributedby pages 12-13).
A yeast two-hybrid assay detected a weak but reproducible Cao1–Atx1 association: 2.84 Miller units versus approximately 0.24 in vector controls. Interaction increased to 6.20 units under TTM-mediated copper limitation, compared with 3.10 under basal conditions and 3.91 with added copper. Altering five basic Atx1 residues impaired the interaction. These results support an Atx1–Cao1 copper-transfer model, although direct metal transfer between purified proteins was not demonstrated (peter2008élucidationdunmécanisme pages 66-70).
Approximately 20–30% residual activity remains without Atx1, indicating another copper-loading route. Deletion of ccc2, cox17, or pccs/ccs1, and disruption of glutathione biosynthesis, did not markedly reduce Cao1 activity under the tested conditions. The alternative carrier therefore remains unidentified (peter2008élucidationdunmécanismea pages 70-73, peter2008élucidationdunmécanisme pages 70-73, peter2008élucidationdunmécanisme pages 73-77).
Copper delivery becomes temporally reorganized during meiotic differentiation. Early in meiosis, cell-surface Ctr4–Ctr5 imports environmental copper. Ctr6 subsequently contributes by mobilizing vacuolar copper, and the meiosis-specific transporter Mfc1 becomes important after approximately six hours, when copper must be accumulated in developing prespores (plante2014characterizationofschizosaccharomyces pages 11-12, plante2014characterizationofschizosaccharomyces pages 13-14).
Plante et al., published April 2014 in Journal of Biological Chemistry, measured CAO activity during synchronous meiosis (https://doi.org/10.1074/jbc.M113.543678). At nine hours, deletion of mfc1 in a ctr4Δ ctr6Δ background reduced CAO activity by 43% relative to the double mutant and by 79% relative to wild type. Cao1 abundance remained comparable among strains, and added copper restored or increased activity, indicating impaired copper loading rather than decreased protein expression (plante2014characterizationofschizosaccharomyces pages 11-12).
These findings support a developmental pathway in which distinct transporters maintain Cao1 metallation as cellular copper sources and compartment architecture change: Ctr4–Ctr5 early, Ctr6 during middle/late stages, and Mfc1 in prespores. This is a copper-distribution pathway, not evidence that Cao1 itself acts as a transporter or signaling protein (plante2014characterizationofschizosaccharomyces pages 11-12, plante2014characterizationofschizosaccharomyces pages 13-14).
The most precise process term is primary-amine catabolism coupled to nitrogen utilization. cao1⁺ is induced by nitrogen limitation, consistent with recruitment of Cao1 when primary amines must serve as nitrogen sources. In contrast, copper chelation, added CuSO₄, or loss of Cuf1 did not materially alter cao1⁺ transcript abundance. Copper regulation is therefore principally post-transcriptional—through cofactor acquisition and enzyme maturation—rather than transcriptional control of cao1 itself (peter2008élucidationdunmécanisme pages 66-70, peter2008élucidationdunmécanismea pages 59-63).
Hydrogen peroxide is an obligatory reaction product, but the retrieved evidence does not establish Cao1 as a dedicated signaling oxidase or quantify its contribution to cellular oxidative stress. Similarly, the meiotic studies use Cao1 activity as a sensitive readout of copper delivery, but they do not demonstrate that Cao1 is the principal driver of meiotic progression. Broad pleiotropic assignments should consequently be avoided.
For S. pombe, Cao1 has two established research applications. First, growth on ethylamine provides a functional genetic assay for Cao1-dependent nitrogen assimilation. Second, CAO activity serves as a biochemical reporter of cytosolic and developmental copper bioavailability, allowing investigators to dissect Ctr4/Ctr5, Ctr6, Mfc1, Cuf1, and Atx1 function (peter2008élucidationdunmécanisme pages 66-70, plante2014characterizationofschizosaccharomyces pages 11-12).
No industrial, diagnostic, therapeutic, or environmental implementation specific to Q9P7F2 was found. Broader copper-amine-oxidase applications should not be automatically assigned to this protein because substrate selectivity, stability, production yield, and purified-enzyme kinetics have not been adequately characterized for Cao1.
Target-specific searches using Q9P7F2, SPAC2E1P3.04, cao1/spao1, the organism, and copper-amine-oxidase terminology did not identify a 2023–2024 primary study focused on this protein. The most informative target-specific mechanistic paper remains Peter et al. (October 2008), while the major developmental extension is Plante et al. (April 2014). Thus, prioritizing recent sources cannot supersede the older direct evidence without risking confusion with unrelated CAO1 symbols or enzymes from other organisms (peter2008copperdistributedby pages 1-2, plante2014characterizationofschizosaccharomyces pages 11-12).
The current evidence supports a high-confidence annotation for reaction class, copper dependence, cytosolic localization, and ethylamine-dependent nitrogen assimilation. Confidence is moderate for the detailed TPQ mechanism because it rests partly on family conservation, and lower for the natural substrate spectrum because no Cao1-specific kinetic constants or metabolomic flux measurements were located. Major unresolved questions are the identity of the Atx1-independent copper carrier, direct structural and spectroscopic validation of Q9P7F2’s TPQ/copper center, quantitative substrate kinetics, and Cao1’s precise spatial organization in mature spores (peter2008élucidationdunmécanismea pages 70-73, peter2008élucidationdunmécanisme pages 73-77, peter2008élucidationdunmécanisme pages 59-63).
References
(peter2008élucidationdunmécanismea pages 59-63): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008copperdistributedby pages 2-2): Chardeen Peter, Julie Laliberté, Jude Beaudoin, and Simon Labbé. Copper distributed by atx1 is available to copper amine oxidase 1 in schizosaccharomyces pombe. Oct 2008. URL: https://doi.org/10.1128/ec.00230-08, doi:10.1128/ec.00230-08. This article has 37 citations and is from a peer-reviewed journal.
(peter2008élucidationdunmécanisme pages 59-63): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008élucidationdunmécanismea pages 70-73): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008élucidationdunmécanisme pages 66-70): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008élucidationdunmécanismea pages 66-70): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008copperdistributedby pages 7-8): Chardeen Peter, Julie Laliberté, Jude Beaudoin, and Simon Labbé. Copper distributed by atx1 is available to copper amine oxidase 1 in schizosaccharomyces pombe. Oct 2008. URL: https://doi.org/10.1128/ec.00230-08, doi:10.1128/ec.00230-08. This article has 37 citations and is from a peer-reviewed journal.
(peter2008copperdistributedby pages 1-2): Chardeen Peter, Julie Laliberté, Jude Beaudoin, and Simon Labbé. Copper distributed by atx1 is available to copper amine oxidase 1 in schizosaccharomyces pombe. Oct 2008. URL: https://doi.org/10.1128/ec.00230-08, doi:10.1128/ec.00230-08. This article has 37 citations and is from a peer-reviewed journal.
(peter2008élucidationdunmécanismea pages 63-66): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008copperdistributedby pages 12-13): Chardeen Peter, Julie Laliberté, Jude Beaudoin, and Simon Labbé. Copper distributed by atx1 is available to copper amine oxidase 1 in schizosaccharomyces pombe. Oct 2008. URL: https://doi.org/10.1128/ec.00230-08, doi:10.1128/ec.00230-08. This article has 37 citations and is from a peer-reviewed journal.
(plante2014characterizationofschizosaccharomyces pages 11-12): Samuel Plante, Raphaël Ioannoni, Jude Beaudoin, and Simon Labbé. Characterization of schizosaccharomyces pombe copper transporter proteins in meiotic and sporulating cells. Apr 2014. URL: https://doi.org/10.1074/jbc.m113.543678, doi:10.1074/jbc.m113.543678. This article has 12 citations and is from a domain leading peer-reviewed journal.
(plante2014characterizationofschizosaccharomyces pages 13-14): Samuel Plante, Raphaël Ioannoni, Jude Beaudoin, and Simon Labbé. Characterization of schizosaccharomyces pombe copper transporter proteins in meiotic and sporulating cells. Apr 2014. URL: https://doi.org/10.1074/jbc.m113.543678, doi:10.1074/jbc.m113.543678. This article has 12 citations and is from a domain leading peer-reviewed journal.
(peter2008élucidationdunmécanisme pages 63-66): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008élucidationdunmécanisme pages 70-73): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.
(peter2008élucidationdunmécanisme pages 73-77): C Peter. Élucidation d'un mécanisme d'acquisition du cuivre par l'amine oxydase cu-dépendante cao1. Unknown journal, 2008.