Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
1. Applicant’s election of Group I (claims 1-29) in the reply filed on 1/23/26 is acknowledged.
If invention I (claims 1-29) is elected, elect:
One specific surface from each of claim 9 and claim 11.
One specific linker from each of claims 12, 14, 16, 17, 21/Table 1 (single sequence from material binding peptide of SEQ ID Nos. 1-131); and one specific linker from each of claims 24, 25 and 28; and [Table 2- election of a single sequence from SEQ ID Nos. 34-51 (conductive peptide) or SEQ ID Nos. 176-180; and a single sequence from SEQ ID Nos. 136-154 (Nanowire peptide).
One specific enzyme from each of claims 4 & 5.
In electing species from (surface, linker & enzyme) it is important to make the election as complete as possible to a single construct.
In response, Applicant elects with traverse as follows:
1) the specific surface from claim 9 is carbon based and claim 11 is carbon felt,
2) One specific linker from each of claims 12, 14, 16, 17, 21/Table 1 (single sequence from material binding peptide of SEQ ID Nos. 1-131; one specific linker from each of claims 24, 25 and 28, and [Table 2- election of a single sequence from SEQ ID Nos. 34-51 (conductive peptide) or SEQ ID Nos. 176-180; and a single sequence from SEQ ID Nos. 136-154, the linker elected is a linker that comprises a peptide such as a material binding peptide (MBP); and
3) One specific enzyme from claims 4 and 5 is Flavoprotein oxidoreductase (claim 5)
that produces hydrogen peroxide (claim 4).
In other words, Applicant elects that the surface is carbon based with a specificity of carbon felt for claim 11; the linker is a peptide, wherein a peptide may include a material binding peptide (see, for example, SEQ ID NO. 25), and the enzyme is a Flavoprotein oxidoreductase that produces hydrogen peroxide.
2. Since Applicants did not elect a specific linker sequence from Table 1 & 2, as required. The first sequence in each of Table 1 & 2; i.e. SEQ ID NO: 1 (from Table 1) and (a) conductive peptide of SEQ ID NO: 34 and (b) Nanowire sequence of SEQ ID NO: 136 will be considered in this examination.
3. Claims withdrawn:
Non-elected species and sequences are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
4. Priority
Applicant’s claim for domestic priority under 35 U.S.C. 119(e), filed 03/07/2005, is acknowledged.
5. The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-29 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
Scope of the claimed genus
1. An enzymatic reactor cell, comprising: a surface, a linker, and one or more enzymes, wherein the surface is directly linked to the linker and the linker is further directly linked to the enzyme, wherein the enzymatic reactor cell produces superoxide and/or hydrogen peroxide.
2. The enzymatic reactor cell of claim 1, wherein the one or more enzymes comprises an enzyme that produces hydrogen peroxide and/or superoxide.
3. The enzymatic reactor cell of claim 2, wherein the enzyme that produces hydrogen peroxide and/or superoxide is a mutant form.
4. The enzymatic reactor cell of claim 2, wherein the enzyme that produces hydrogen peroxide and/or superoxide may also produce another product, such as the enzyme glucose oxidase, alcohol oxidase, formate oxidase, sulfite oxidase, alditol oxidase, pyruvate oxidase, lactate oxidase, amine oxidase, glycolate oxidase or combinations thereof.
5. The enzymatic reactor cell of claim 2, wherein the enzyme that produces hydrogen peroxide and/or superoxide is methane monooxygenase reductase subunit, a flavoprotein oxidoreductase, an NADH Oxidase and/or NAD(P)H oxidase.
6. The enzymatic reactor cell of claim 5, wherein the enzyme is an NADH Oxidase and/or a flavoprotein oxidoreductase from Table 4.
7. The enzymatic reactor cell of claim 1, wherein the enzymatic reactor cell further comprises a starting agent or starting substrate that is oxygen, and the oxygen source is oxygen gas, dissolved oxygen, from air or specifically, compressed air, or combinations thereof.
8. The enzymatic reactor cell of claim 1, wherein the surface is an electrode.
9. The enzymatic reactor cell of claim 1, wherein the surface is carbon based, an inorganic surface, a metal, a metal oxide, silica or silicon, comprises a polymer such as cellulose, polystyrene, PDMS, chlorine doped polypyrrole, polypropylene, is an alloy and/or is a combination thereof.
10. The enzymatic reactor cell of claim 9, wherein the surface is carbon based.
11. The enzymatic reactor cell of claim 10, wherein the carbon based surface comprises one or more from the following: graphite; graphene; Glassy carbon; Carbon/graphite felt; carbon/graphite paper; teflonated carbon paper; teflonated carbon felt; carbon based gas diffusion electrode containing a macroporous and/or microporous layer; SWCNT; MWCNT; activated carbon; graphite foil; Carbon nanofibers; Carbon nanotubes; Carbon black-coated graphite felt; Microporous carbon; Hierarchically porous carbon; and/or Mesoporous carbon; heteroatom doped carbon (e.g., oxygen/nitrogen/boron/sulphur/fluorine/—COOH/C—O—C doped carbon, oxidized graphite felt, oxygenated carbon nanotubes, quinone incorporated carbon nanostructures, edge oxygenated graphitic nanoplatelets, or nitrogen-rich layered graphene.
12. The enzymatic reactor cell of claim 1, wherein the linker comprises a peptide, protein, a chemical polymer, and/or polynucleotide.
13. The enzymatic reactor cell of claim 1, wherein the linker comprises a surface binding moiety (SBM).
14. The enzymatic reactor cell of claim 13, wherein the surface binding moiety (SBM) binds to or is immobilized to the surface, another portion of the linker, and/or the enzyme by non-covalent bonding, covalent bonding, physisorption, and/or high affinity binding.
15. The enzymatic reactor cell of claim 13, wherein the surface binding moiety (SBM) is covalently bonded to the surface, another portion of the linker, and/or the enzyme.
16. The enzymatic reactor cell of claim 15, wherein the surface binding moiety (SBM) is covalently bonded to the surface, another portion of the linker, and/or the enzyme by click chemistry, dithiol bond formation, Michael addition, nucleophilic substitution, a metal-sulfur bond linkage, a metal-nitrogen bond linkage, a metal-oxygen bond linkage, enzyme catalyzed conjugation, and/or EDC coupling.
17. The enzymatic reactor cell of claim 15, wherein the surface binding moiety (SBM) is covalently bonded by continuous protein expression wherein the surface binding moiety (SBM) is a continuous protein with another portion of the linker; the surface binding moiety (SBM) is a continuous protein with the enzyme; or the surface binding moiety (SBM) is a continuous protein with another portion of the linker, and/or the enzyme.
18. The enzymatic reactor cell of claim 1, wherein the linker binds to another portion of the linker, the enzyme, and/or the surface.
19. The enzymatic reactor cell of claim 18, wherein the linker is covalently bonded to another portion of the linker, the enzyme, and/or the surface by click chemistry, dithiol bond formation, Michael addition, nucleophilic substitution, a metal-sulfur bond linkage, a metal-nitrogen bond linkage, a metal-oxygen bond linkage, enzyme catalyzed conjugation, and/or EDC coupling.
20. The enzymatic reactor cell of any claim 13, wherein the SBM comprises a material binding peptide (MBP).
21. The enzymatic reactor cell of claim 20, wherein the material binding peptide (MBP) or surface binding moiety (SBM) of the linker comprises an amino acid sequence from Table 1.
22. The enzymatic reactor cell of claim 20, wherein the material binding peptide (MBP) binds to carbon base surfaces, metal, metal oxide, a polymer and/or an inorganic surface.
23. The enzymatic reactor cell of claim 20, wherein the MBP comprises SEQ ID NO. 25.
24. The enzymatic reactor cell of claim 1, wherein the linker comprises a peptide, protein, a chemical polymer, nanowire, polynucleotide or chemical means such as chemical nanowires to link a) portions of the linker together, b) the linker to the surface and/or c) the linker to the enzyme.
25. The enzymatic reactor cell of claim 24, wherein the chemical means or chemical nanowire may use for linking, or include a maleimide functional group, a tetrafluorophenyl functional group, an aldehyde functional group, an amine functional group, a N-hydroxysuccinimide functional group, a thiol functional group, a haloacetyl functional group, a pyridyl disulfide functional group, an imidoester functional group, an epoxide functional group, a hydrocarbon chain, one of more polyethylene glycol units, and/or one or more aromatic rings.
26. The enzymatic reactor cell of claim 24, wherein the nanowire comprises or uses maleimide.
27. The enzymatic reactor cell of claim 24, wherein the linker comprises a peptide or protein.
28. The enzymatic reactor cell of claim 27, wherein the peptide or protein comprises an amino acid sequence from Table 2 or SEQ ID NO: 176-180.
29. A method of performing an enzymatic reaction or enzymatic pathway with the use of an enzymatic reactor cell of claim 1 or a plurality of enzymatic reactor cells of claim 1.
The subject of this rejection is the recitation in:
Claims 1-4 (for example) - An enzymatic reactor cell, comprising: a surface, a linker, and one or more enzymes, wherein the surface is directly linked to the linker and the linker is further directly linked to the enzyme, wherein the enzymatic reactor cell produces superoxide and/or hydrogen peroxide.
2. The enzymatic reactor cell of claim 1, wherein the one or more enzymes comprises an enzyme that produces hydrogen peroxide and/or superoxide.
3. The enzymatic reactor cell of claim 2, wherein the enzyme that produces hydrogen peroxide and/or superoxide is a mutant form.
4. The enzymatic reactor cell of claim 2, wherein the enzyme that produces hydrogen peroxide and/or superoxide may also produce another product, such as the enzyme glucose oxidase, alcohol oxidase, formate oxidase, sulfite oxidase, alditol oxidase, pyruvate oxidase, lactate oxidase, amine oxidase, glycolate oxidase or combinations thereof.
The claims encompass any enzymatic reactor cell construct, and comprising: any surface, any linker, and any enzyme (or mutant form thereof as in claims 1-3) that produces hydrogen peroxide and/or superoxide; or may also produce any another product, wherein the the enzyme glucose oxidase, alcohol oxidase, formate oxidase, sulfite oxidase, alditol oxidase, pyruvate oxidase, lactate oxidase, amine oxidase, glycolate oxidase or combinations thereof – from any source. Further genus is inclusive of the method claim - 29. A method of performing any enzymatic reaction or any enzymatic pathway with the use of an enzymatic reactor cell of claim 1 or a plurality of enzymatic reactor cells of claim 1. Further claims 6-28 list a variety of surfaces, linkers and enzymes which appear to more a review of literature rather than concrete bases for the specific invention.
Assessment of whether species are disclosed in the original specification
The Specification only describes specific instances in which an enzymatic reactor cell, comprising: an stainless steel electrode surface, a linker, and one or more enzymes, wherein the electrode surface is directly linked to the linker and the linker is further directly linked to one of the one or more enzymes, wherein the linker comprises a surface binding moiety (SBM) immobilized to the electrode surface and/or one of the one or more enzymes, and wherein the SBM comprises a material binding peptide (MBP) comprising a sequence selected from the group consisting of: (i) SEQ ID NO: 25, SEQ ID NO: 104; (ii) nanowire sequence of SEQ ID NO: 136; and (iii) and enzyme from Thermus thermophilus HB27 NADH Oxidase; fusion as SEQ ID NO: 156, or SEQ ID NO: 157 or SEQ ID NO: 158 to produce H2O2. See PG Pub. US 20250346929 of the instant application, paragraphs [0155, 0162, 0159].
Assessment of whether disclosed species are representative of the claimed genus
MPEP § 2163 states that a representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
In the instant case, the Specification describes enzymatic reactor cell which is a combination of SBM comprises a material binding peptide (MBP) comprising a sequence selected from the group consisting of: (i) SEQ ID NO: 25, SEQ ID NO: 104; (ii) nanowire sequence of SEQ ID NO: 136; and (iii) and enzyme from Thermus thermophilus HB27 NADH Oxidase; fusion as SEQ ID NO: 155, 156, or SEQ ID NO: 157 or SEQ ID NO: 158 to produce H2O2. See PG Pub. US 20250346929 of the instant application, paragraphs [0155, 0162, 0159]. The Specification, however, does not describe any enzymatic reactor cell, comprising: any surface, any linker, and any enzymes, wherein the surface is directly linked to the linker and the linker is further directly linked to the enzyme, wherein the enzymatic reactor cell produces superoxide and/or hydrogen peroxide.
In the alternate, the description does not disclose the invention in a manner sufficiently clear and complete to be carried out by a person skilled in the art. In contrast to the breadth of the claims, the description does not appear to disclose and enable an enzymatic reactor cell comprising of enzymes, surfaces and linkers other than the following: an NADH oxidase from Thermus thermophilus HB27 having the amino acid sequence set forth in SEQ ID NO. 155-158 on either a steel or carbon surface, immobilized by a linker consisting of a material binding peptide (MBP) having the amino acid sequence of either SEQ ID Nos. 104 or 25 and the peptide nanowire 9 (SEQ ID NO. 136) (Examples 5-8). Specifically with regards to the linker (claims 30, 31, 38, 39, 44 and 45), the description does not appear to fully disclose and enable a non-peptide linker, i.e. a linker comprising either chemical means or a DNA nanowire. Although non-peptide linkers (paras. [00106]-[00107], Table 3) and other peptide linkers (Table 2) are contemplated in the description, the amount of direction provided is insufficient to enable the skilled person to incorporate such linkers without undue experimentation. Examples 5-8 in the description are limited to a linker consisting of specific MBPs and a specific peptide nanowire, as discussed above.
Identifying characteristics and structure/function correlation
In the absence of a reduction to practice of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. To meet this requirement in the instant case, the specification must describe the structural, physical and/or chemical properties of enzymatic reactor cell construct and the functional characteristics of cell construct as outlined above.
Accordingly, the specification fails to provide guidance on the specific structural features of the genus that account for the function of the genus, namely what portions and variations of reactor cell construct including the structural features as described in the in the instant specification that would allow for production of superoxide and/or hydrogen peroxide. Absent this information, the skilled artisan cannot readily envisage specific embodiments of reactor cell construct that possess the relevant functional properties.
In conclusion, the skilled artisan would not reasonably conclude that the inventor(s), at the time the application was filed, had possession of the full scope of the invention with respect to any enzymatic reactor cell, comprising: a surface, a linker, and one or more enzymes, wherein the surface is directly linked to the linker and the linker is further directly linked to the enzyme, wherein the enzymatic reactor cell produces superoxide and/or hydrogen peroxide
6. Claim Rejections - 35 USC § 112 (second paragraph)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 6, 21 & 28 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claims 6, 21 & 28 recite – Tables 4, 1 & 2 respectively which are indefinite.
Applications which include tables with large numbers of genes, proteins, small molecule biomarkers, diseases, acceptable excipients, etc. Claims cannot refer back to these tables in the specification; e.g., "wherein the biomarkers are selected from the group consisting of those listed in Table 4" or "wherein the cancer is one of those listed in Table 3." Claims such as these are rejected under §112(b), and Applicants instructed to copy the table contents into the claim itself. There is no limit to the length of a claim. If the subject matter can be listed in the specification, that list can be copied and pasted into a claim.
7. Claims 4-6, 9-11 & 24-27 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claim 4 recites:
4. The enzymatic reactor cell of claim 2, wherein the enzyme that produces hydrogen peroxide and/or superoxide may also produce another product, such as the enzyme glucose oxidase, alcohol oxidase, formate oxidase, sulfite oxidase, alditol oxidase, pyruvate oxidase, lactate oxidase, amine oxidase, glycolate oxidase or combinations thereof.
It is unclear how an enzyme that produces hydrogen peroxide and/or superoxide may also produce another product – which is an enzyme.
Claims 4, 9 & 24 recite the words ‘such as’. The use of the expressions “preferably”, “substantially”, “optionally”, “close to”, “such as” (claims 4, 9 & 24), and “substantial” attempts to give both broad and narrow meaning to the scope of the claims. These claims are unclear.
Claims 5-6, 10-11 & 25-27 are included in the rejection for failing to correct the defect present in the base claim(s).
8. In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 1-12 & 15 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by ROCHA-MARTIN J., et al. "New biotechnological perspectives of a NADH oxidase variant from Thermus thermophilus HB27 as NAD+-recycling enzyme". BMC Biotechnol, 3 November 2011, Vol. 11, pages 1-11.
ROCHA-MARTIN J., et al. teaches an NADH oxidase variant from Thermus thermophilus HB27 (NOX) chemically linked to a non-electrode polymeric surface, wherein the combination produces hydrogen peroxide (See Abstract, pages 2-3, 7-9). Specifically, NOX was immobilized through different chemistries onto agarose, including through covalent attachment to glyoxyl groups (an aldehyde functional group) (page 5, left column). The amino acid sequence of said NADH oxidase is identical to that set forth in present SEQ ID NO. 155. Thus the reference teaches an enzymatic reactor cell construct, comprising: a surface, a linker, and an enzymes. Noting above in paragraph 5, that the claims are written so broadly and not described as per the specification provided, claims 1-12, and 15 are anticipated by the cited reference.
9. Double Patenting Rejection
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the claims at issue are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); and In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP §§ 706.02(l)(1) - 706.02(l)(3) for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
Effective January 1, 1994, a registered attorney or agent of record may sign a terminal disclaimer. A terminal disclaimer signed by the assignee must fully comply with 37 CFR 3.73(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/forms/. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to http://www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 1-29 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-32 of U.S. Patent No. 12,516,311 B2. Although the claims at issue are not identical, they are not patentably distinct from each other because of the following reason(s).
Instant claims 1-29 are presented above in paragraph above 6.
Instant claims 1-32 are presented as follows:
1. An enzymatic reactor cell, comprising: an electrode surface, a linker, and one or more enzymes, wherein the electrode surface is directly linked to the linker and the linker is further directly linked to one of the one or more enzymes, wherein the linker comprises a surface binding moiety (SBM) immobilized to the electrode surface and/or one of the one or more enzymes, and wherein the SBM comprises a material binding peptide (MBP) comprising a sequence selected from the group consisting of: (i) SEQ ID NO: 14, SEQ ID NO: 3, SEQ ID NO: 25, SEQ ID NO: 17, SEQ ID NO: 20, or SEQ ID NO: 50; (ii) sequences having at least 99% sequence identity to SEQ ID NO: 14; and (iii) sequences having at least 75% sequence identity to SEQ ID NO: 3, SEQ ID NO: 25, SEQ ID NO: 17, SEQ ID NO: 20, or SEQ ID NO: 50.
2. The enzymatic reactor cell of claim 1, wherein the enzymatic reactor cell has the following Formula II:
[electrode surface-surface linker-enzyme].sub.n(1-10) (Formula II); wherein when n is 2-10, each [electrode surface-surface linker-enzyme] comprises a different electrode surface, surface linker and/or enzyme from the other [electrode surface-surface linker-enzyme].
3. The enzymatic reactor cell of claim 1, wherein the electrode surface is a metal, a polymer, a biological surface and/or crystalline.
4. The enzymatic reactor cell of claim 3, wherein the electrode surface comprises graphite, graphene, glassy carbon, carbon paper, carbon felt, platinum, titanium, a metal oxide, cellulose, polystyrene, silica, gold, gold alloy, gold palladium alloy, or a combination thereof, wherein the metal oxide is zinc oxide, iron oxide, titanium oxide, or manganese oxide.
5. The enzymatic reactor cell of claim 4, wherein the electrode surface is planar, non-planar, spherical, in the shape of nanoparticles, disc-shaped, an aerogel, and/or fibrous.
6. The enzymatic reactor cell of claim 1, wherein the electrode surface is the anode and/or the cathode.
7. The enzymatic reactor cell of claim 1, wherein the linker comprises the SBM and a peptide, a protein, a chemical, a chemical polymer, a nanowire, or a polynucleotide.
8. The enzymatic reactor cell of claim 7, wherein the linker comprises a nanowire, and the nanowire is a chemical nanowire that (i) comprises glutaraldehyde, SMCC (Succinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxylate), TFP-dPEG.sub.2Mal, MBS (m-maleimido-benzoyl-N-hydroxysuccinimide ester), bis-MAL-dPEG.sub.3, or a maleimide, or (ii) uses glutaraldehyde, SMCC (Succinimidyl 4-(N-maleimidomethyl) cyclohexane-1-carboxylate), TFP-dPEG.sub.2Mal, MBS (m-maleimidobenzoyl-N-hydroxysuccinimide ester), bis-MAL-dPEG.sub.3, or a maleimide for linking a) the SBM and/or one or more peptides, proteins, chemicals, chemical polymers, nanowires, or polynucleotides together, b) the linker to the electrode surface, and/or c) the linker to the enzyme.
9. The enzymatic reactor cell of claim 7, wherein the linker comprises a nanowire, and the nanowire is a single or double stranded DNA nanowire, wherein the single or double stranded DNA nanowire comprises a sequence selected from the group consisting of SEQ ID NOs: 86-89.
10. The enzymatic reactor cell of claim 7, wherein the linker comprises a peptide sequence comprising a sequence selected from the group consisting of SEQ ID NOs: 34-49, and 51.
11. The enzymatic reactor cell of claim 7, wherein the SBM is immobilized to a) the electrode surface, b) the peptide, protein, chemical, chemical polymer, nanowire, or polynucleotide, and/or (c) the enzyme by non-covalent bonding, covalent bonding, physisorption, and/or high affinity binding.
12. The enzymatic reactor cell of claim 1, wherein the MBP comprises SEQ ID NO: 25.
13. The enzymatic reactor cell of claim 1, wherein the enzymatic reactor cell comprises one enzyme and performs a single enzymatic reaction in said enzymatic reactor cell.
14. The enzymatic reactor cell of claim 1, wherein the enzymatic reactor cell comprises more than one enzyme and performs more than one enzymatic reaction in said enzymatic reactor cell.
15. The enzymatic reactor cell of claim 1, wherein the enzyme comprises a sequence selected from SEQ ID NOs: 80-85.
16. The enzymatic reactor cell of claim 1, wherein the enzymatic reactor cell comprises a wildtype or mutant form of formate dehydrogenase, formaldehyde dehydrogenase, and/or alcohol dehydrogenase.
17. The enzymatic reactor cell of claim 16, wherein the enzymatic reactor cell comprises a wildtype or mutant form of formate dehydrogenase.
18. The enzymatic reactor cell of claim 17, wherein the enzymatic reactor cell comprises a mutant form of formate dehydrogenase.
19. The enzymatic reactor cell of claim 1, wherein the enzymatic reactor cell further comprises one or more starting agents or substrates, and wherein the starting agent or substrate is carbon dioxide, formic acid, and/or formaldehyde.
20. The enzymatic reactor cell of claim 19, wherein the enzymatic reactor cell produces formate, formic acid, formaldehyde, and/or methanol.
21. The enzymatic reactor cell of claim 1, wherein the enzyme is an oxidoreductase enzyme.
22. The enzymatic reactor cell of claim 1, wherein the SBM is immobilized to the electrode surface and/or the enzyme by non-covalent bonding, covalent bonding, physisorption, and/or high affinity binding.
23. The enzymatic reactor cell of claim 22, wherein the SBM is covalently bonded by click chemistry, dithiol bond formation, Michael addition, nucleophilic substitution, a metal-sulfur bond linkage, or enzyme catalyzed conjugation.
24. The enzymatic reactor cell of claim 1, wherein the SBM is immobilized to the electrode surface by high affinity non-covalent binding.
25. The enzymatic reactor cell of claim 7, wherein the SBM is immobilized to (a) the electrode surface, (b) the peptide, protein, chemical, chemical polymer, nanowire, or polynucleotide, and/or (c) the enzyme.
26. The enzymatic reactor cell of claim 25, wherein the SBM is immobilized to the electrode surface by high affinity non-covalent binding.
27. The enzymatic reactor cell of claim 7, wherein the linker comprises streptavidin and/or a biotinylated peptide/protein for linkage to the SBM or linkage to the enzyme, wherein the enzyme is optionally biotinylated.
28. The enzymatic reactor cell of claim 11, wherein the SBM is covalently bonded by click chemistry, dithiol bond formation, Michael addition, nucleophilic substitution, a metal-sulfur bond linkage, or enzyme catalyzed conjugation.
29. The enzymatic reactor cell of claim 28, wherein the SBM is a continuous protein with (a) the peptide or protein the, (b) with the enzyme, or (c) with the peptide or protein and the enzyme.
30. An enzymatic reactor cell, comprising: an electrode surface, a linker, and one or more enzymes, wherein the electrode surface is directly linked to the linker and the linker is further directly linked to one of the one or more enzymes, wherein the linker comprises: i) a peptide, a protein, a chemical, a chemical polymer, a nanowire, or a polynucleotide that links a) one or more peptides, proteins, chemicals, chemical polymers, nanowires, or polynucleotides of the linker together, b) the linker to the electrode surface and/or c) the linker to the enzyme; and ii) a peptide sequence of SEQ ID NO: 51.
31. A method of performing an enzymatic reaction or enzymatic pathway with the use of an enzymatic reactor cell of claim 1.
32. A method of performing an enzymatic reaction or enzymatic pathway with the use of a plurality of enzymatic reactor cells of claim 1.
Given the fact pattern of the instant case as well as the patent the species claims of the patent anticipates and make obvious the instant genus (or broad) claims. Patented claims are drawn to specific enzymatic reactor cell construct that is capable producing any product. Further, as noted in the applied patent – [61] the reactor cells or a single reactor cell, can include multiple types of surfaces or multiple types of linker or electrode surface linkers, and/or multiple enzymes. For example, a single reactor cell can include more than one enzyme from an enzymatic pathway, wherein the different enzymes in the pathway are attached to the surface of the reactor cell. Therefore, one skilled in the art would have a reason success of employing any of the multiple enzymes to produce superoxide and/or hydrogen peroxide.
10. No claim is allowed.
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/TEKCHAND SAIDHA/
Primary Examiner, Art Unit 1652
Recombinant Enzymes, Hoteling
Telephone: (571) 272-0940
Fax: (571) 273-0940