[ { "id": "https://authors.library.caltech.edu/records/rrbjb-76q78", "eprint_id": 115868, "eprint_status": "archive", "datestamp": "2023-08-20 08:12:59", "lastmod": "2023-10-24 20:54:16", "type": "monograph", "metadata_visibility": "show", "creators": { "items": [ { "id": "McNicholas-Brendon-J", "name": { "family": "McNicholas", "given": "Brendon J." }, "orcid": "0000-0002-3654-681X" }, { "id": "Nie-Cherish", "name": { "family": "Nie", "given": "Cherish" } }, { "id": "Jose-Anex", "name": { "family": "Jose", "given": "Anex" } }, { "id": "Oyala-Paul-H", "name": { "family": "Oyala", "given": "Paul H." }, "orcid": "0000-0002-8761-4667" }, { "id": "Takase-Michael-K", "name": { "family": "Takase", "given": "Michael K." }, "orcid": "0000-0001-8365-3645" }, { "id": "Henling-Larry-M", "name": { "family": "Henling", "given": "Larry M." } }, { "id": "Barth-Alexandra-T", "name": { "family": "Barth", "given": "Alexandra T." }, "orcid": "0000-0002-1813-4029" }, { "id": "Amaolo-Alessio", "name": { "family": "Amaolo", "given": "Alessio" } }, { "id": "Hadt-R-G", "name": { "family": "Hadt", "given": "Ryan G." }, "orcid": "0000-0001-6026-1358" }, { "id": "Solomon-Edward-I", "name": { "family": "Solomon", "given": "Edward I." }, "orcid": "0000-0003-0291-3199" }, { "id": "Winkler-Jay-R", "name": { "family": "Winkler", "given": "Jay R." }, "orcid": "0000-0002-4453-9716" }, { "id": "Gray-H-B", "name": { "family": "Gray", "given": "Harry B." }, "orcid": "0000-0002-7937-7876" }, { "id": "Despagnet-Ayoub-Emmanuelle", "name": { "family": "Despagnet-Ayoub", "given": "Emmanuelle" }, "orcid": "0000-0002-9013-7574" } ] }, "title": "Boronated Cyanometallates", "ispublished": "unpub", "full_text_status": "public", "note": "The content is available under CC BY NC ND 4.0 License. \n\nWe dedicate this paper to the memory of Bob Grubbs, a great scientist and dear friend, who urged (ordered!) three of us (H.B.G., B.J.M., E.D.A.) to develop new redox complexes for use in nonaqueous redox flow batteries. After considering various options, we began work on boronated cyanometallates. We acknowledge the X-ray Crystallography Facility in the Beckman Institute at Caltech, and the Dow Next Generation Instrumentation Grant for X-ray structure collection. R.G.H. gratefully acknowledges financial support from Caltech and the Dow Next Generation Educator Fund. EPR spectroscopy was performed in the Caltech EPR facility, which is also supported by the Beckman Institute and the Dow Next Generation Educator Fund. We thank David van der Velde for assistance in interpreting NMR data. We thank Wesley Kramer and Brian Sanders for helpful discussions. The computations presented here were conducted in the Resnick High Performance Computing Center, a facility supported by Resnick Sustainability Institute at the California Institute of Technology. \n\nThis work was supported by the National Science Foundation (CHE-1763429). Additional funding was provided by two Arthur A. Noyes SURF Fellowships (C. N. and A. A.) and the Beckman Institute Laser Resource Center supported by the Arnold and Mabel Beckman Foundation. \n\nAuthor Contributions. All authors have given approval to the final version of the manuscript.\n\n
Submitted - boronated-cyanometallates.pdf
Supplemental Material - boronated-cyanometallates-supporting-information.pdf
", "abstract": "Fourteen boronated cyanometallates ([M(CN-BR\u2083)\u2086]^(3/4/5\u2013) (M = Cr, Mn, Fe, Ru, Os, R = BPh\u2083, B(2,4,6,-F\u2083C\u2086H\u2082)\u2083, B(C\u2086F5)\u2083) have been characterized by X-ray crystallography and spectroscopy [UV-vis-NIR, NMR, IR, spectroelectrochemistry, and magnetic circular dichroism (MCD)]; CASSCF+NEVPT2 methods were employed in calculations of electronic structures. For (t_(2g))\u2075 electronic configurations, the lowest energy ligand-to-metal charge transfer (LMCT) absorptions and MCD C terms in the spectra of boronated species have been assigned to transitions from cyanide \u03c3+\u03c0 + B-C borane \u03c3 orbitals. CASSCF+NEVPT2 calculations including t1u and t2u orbitals reproduced t_(1u)/t_(2u) \u2192 t_(2g) excitation energies. All ([M(CN-BR3)6]3/4\u2212 complexes exhibited highly electrochemically reversible redox couples. Notably, the formal potentials of all five [M(CN-B(C\u2086F\u2085)\u2083)\u2086]\u00b3\u207b anions scale with LMCT energies; and Mn(I) and Cr(II) compounds, (K(18-crown-6))\u2085[Mn(CN-B(C6F\u2085)\u2083)\u2086] and (TBA)\u2084[Cr(CN-B(C\u2086F\u2085)\u2083)\u2086], are surprisingly stable. Continuous wave and pulsed electron paramagnetic resonance (hyperfine sublevel correlation) spectra were collected for all Cr(III) complexes; as expected, \u00b9\u2074N hyperfine splittings are greater for (TBA)\u2083[Cr(NC-BPh\u2083)\u2086] than for (TBA)\u2083[Cr(CN-BPh\u2083)\u2086]. Using (TBA)\u2084[Fe(CN-B(C\u2086F\u2085)\u2083)\u2086] and (TBA)\u2083[Fe(CN)\u2086], a model flow battery was constructed and found to have an 80% energy efficiency.", "date": "2022-07-27", "date_type": "published", "id_number": "CaltechAUTHORS:20220726-998148000", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20220726-998148000", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NSF", "grant_number": "CHE-1763429" }, { "agency": "Dow Next Generation Educator Fund" }, { "agency": "Caltech Beckman Institute" }, { "agency": "Caltech Summer Undergraduate Research Fellowship (SURF)" } ] }, "local_group": { "items": [ { "id": "Resnick-Sustainability-Institute" } ] }, "doi": "10.26434/chemrxiv-2022-8r90r", "primary_object": { "basename": "boronated-cyanometallates.pdf", "url": "https://authors.library.caltech.edu/records/rrbjb-76q78/files/boronated-cyanometallates.pdf" }, "related_objects": [ { "basename": "boronated-cyanometallates-supporting-information.pdf", "url": "https://authors.library.caltech.edu/records/rrbjb-76q78/files/boronated-cyanometallates-supporting-information.pdf" } ], "resource_type": "monograph", "pub_year": "2022", "author_list": "McNicholas, Brendon J.; Nie, Cherish; et el." }, { "id": "https://authors.library.caltech.edu/records/rvt7n-tm718", "eprint_id": 115692, "eprint_status": "archive", "datestamp": "2023-08-20 05:35:58", "lastmod": "2023-10-24 16:40:56", "type": "monograph", "metadata_visibility": "show", "creators": { "items": [ { "id": "Ghosh-Shirsendu", "name": { "family": "Ghosh", "given": "Shirsendu" }, "orcid": "0000-0002-0820-9349" }, { "id": "Banerjee-Ghosh-Koyel", "name": { "family": "Banerjee Ghosh", "given": "Koyel" }, "orcid": "0000-0002-1376-5198" }, { "id": "Levy-Dorit", "name": { "family": "Levy", "given": "Dorit" } }, { "id": "Scheerer-David", "name": { "family": "Scheerer", "given": "David" }, "orcid": "0000-0002-6641-6629" }, { "id": "Riven-Inbal", "name": { "family": "Riven", "given": "Inbal" }, "orcid": "0000-0002-8268-1377" }, { "id": "Shin-Jieun", "name": { "family": "Shin", "given": "Jieun" }, "orcid": "0000-0003-3817-6282" }, { "id": "Gray-H-B", "name": { "family": "Gray", "given": "Harry B." }, "orcid": "0000-0002-7937-7876" }, { "id": "Naaman-Ron", "name": { "family": "Naaman", "given": "Ron" }, "orcid": "0000-0003-1910-366X" }, { "id": "Haran-Gilad", "name": { "family": "Haran", "given": "Gilad" }, "orcid": "0000-0003-1837-9779" } ] }, "title": "Control of protein activity by photoinduced spin polarized charge reorganization", "ispublished": "unpub", "full_text_status": "public", "note": "The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license. \n\nS.G. and K.B.-G. contributed equally to this work. \n\nThis work was partially supported by a grant to G.H. from the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation program (grant agreement No 742637, SMALLOSTERY), a grant from the Israel Science Foundation (no. 1250/19) and a grant from the Weizmann SABRA - Yeda-Sela \u2013 WRC program. G.H. holds the Hilda Pomeraniec Memorial Professorial Chair. R.N. acknowledges partial support from the MINERVA Foundation and from the Israel Ministry of Science and Technology. Work at Caltech was supported by the United States NIH (R01 DK019038 to H.B.G.). \n\nAuthor Contributions: S.G. and K.B.-G. designed the project, performed all experiments and analyzed the results, D.L. prepared labeled proteins, D.S. instructed and participated in enzyme kinetics experiments, J.S. and H.B.G provided materials, G.H. and R.N. conceived and supervised the research and wrote the paper with help from all authors. \n\nThe authors have declared no competing interest.\n\nSubmitted - 2021.10.12.464058v2.full.pdf
", "abstract": "Considerable electric fields are present within living cells, and the role of bioelectricity has been well established at the organismal level. Yet little is known about electric-field effects on protein function. Here we use phototriggered charge injection from a site-specifically attached ruthenium photosensitizer to directly demonstrate the effects of charge redistribution within a protein. We find that binding of an antibody to phosphoglycerate kinase (PGK) is increased two folds under illumination. Remarkably, illumination is found to suppress the enzymatic activity of PGK by a factor as large as three. These responses are sensitive to the photosensitizer position on the protein. Surprisingly, left (but not right) circularly polarized light elicits these responses, indicating that the electrons involved in the observed dynamics are spin polarized, due to spin filtration by protein chiral structures. Our results directly establish the contribution of electrical polarization as an allosteric signal within proteins. Future experiments with phototriggered charge injection will allow delineation of charge rearrangement pathways within proteins and will further depict their effects on protein function.", "date": "2022-07-22", "date_type": "published", "id_number": "CaltechAUTHORS:20220720-917086000", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20220720-917086000", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "European Research Council (ERC)", "grant_number": "742637" }, { "agency": "Israel Science Foundation", "grant_number": "1250/19" }, { "agency": "Weizmann SABRA - Yeda-Sela \u2013 WRC program" }, { "agency": "Hilda Pomeraniec Memorial Professorial Chair" }, { "agency": "MINERVA (Israel)" }, { "agency": "Ministry of Science and Technology (Israel)" }, { "agency": "NIH", "grant_number": "R01 DK019038" } ] }, "doi": "10.1101/2021.10.12.464058", "primary_object": { "basename": "2021.10.12.464058v2.full.pdf", "url": "https://authors.library.caltech.edu/records/rvt7n-tm718/files/2021.10.12.464058v2.full.pdf" }, "resource_type": "monograph", "pub_year": "2022", "author_list": "Ghosh, Shirsendu; Banerjee Ghosh, Koyel; et el." }, { "id": "https://authors.library.caltech.edu/records/bsd7r-k4525", "eprint_id": 109656, "eprint_status": "archive", "datestamp": "2023-08-22 05:42:05", "lastmod": "2023-10-23 18:06:29", "type": "monograph", "metadata_visibility": "show", "creators": { "items": [ { "id": "Garza-L\u00f3pez-Roberto-A", "name": { "family": "Garza-L\u00f3pez", "given": "Roberto A." }, "orcid": "0000-0002-9363-1842" }, { "id": "Kozak-John-J", "name": { "family": "Kozak", "given": "John J." } }, { "id": "Gray-H-B", "name": { "family": "Gray", "given": "Harry B." }, "orcid": "0000-0002-7937-7876" } ] }, "title": "Copper(II) Inhibition of the SARS-CoV-2 Main Protease", "ispublished": "unpub", "full_text_status": "public", "keywords": "SARS-CoV-2; Main Protease; Inhibition; Copper(II) ligands; Mpro; HIS 41; CYS 145; 6LU7; 6VXX; Homodimer; Schiff base; AutoDock Vina; Spike Protein; Spike glycoprotein", "note": "The content is available under CC BY NC ND 4.0 License.\n\nJul 21, 2020 Version 1.\n\nWork at Caltech was supported by the Arnold and Mabel Beckman Foundation. Support at\nPomona College was provided by the Howard Hughes Medical Institute Research Program and a\nSontag Research Fellowship Award. Molecular graphics and analyses performed with UCSF\nChimera, developed by the Resource for Biocomputing, Visualization, and Informatics at the\nUniversity of California, San Francisco, with support from NIH P41-GM103311. Molecular\ngraphics and analyses performed with UCSF ChimeraX, developed by the Resource for\nBiocomputing, Visualization, and Informatics at the University of California, San Francisco,\nwith support from National Institutes of Health R01-GM129325 and the Office of Cyber\nInfrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.\n\nThe author(s) have declared they have no conflict of interest with regard to this content.\n\nThe author(s) have declared ethics committee/IRB approval is not relevant to this content.\n\nSubmitted - copper-ii-inhibition-of-the-sars-co-v-2-main-protease.pdf
", "abstract": "In an analysis of the structural stability of the coronavirus main protease (Mpro), we identified regions of the protein that could be disabled by cobalt(III)-cation binding to histidines and cysteines [1]. Here we have extended our work to include copper(II) chelates, which we have docked to HIS 41 and CYS 145 in the Mpro active-site region. We have found stable docked structures where Cu(II) could readily bond to the CYS 145 thiolate, which would be lethal to the enzyme. We also started studying the Spike Protein, PDB ID: 6VXX and the region around the D614G mutant.", "date": "2021-06-29", "date_type": "published", "publisher": "American Chemical Society", "id_number": "CaltechAUTHORS:20210629-204239084", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20210629-204239084", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Arnold and Mabel Beckman Foundation" }, { "agency": "Howard Hughes Medical Institute (HHMI)" }, { "agency": "Sontag Foundation" }, { "agency": "NIH", "grant_number": "P41-GM103311" }, { "agency": "NIH", "grant_number": "R01-GM129325" }, { "agency": "National Institute of Allergy and Infectious Diseases" } ] }, "local_group": { "items": [ { "id": "COVID-19" } ] }, "doi": "10.26434/chemrxiv.12673436.v1", "pmcid": "PMC7668746", "primary_object": { "basename": "copper-ii-inhibition-of-the-sars-co-v-2-main-protease.pdf", "url": "https://authors.library.caltech.edu/records/bsd7r-k4525/files/copper-ii-inhibition-of-the-sars-co-v-2-main-protease.pdf" }, "resource_type": "monograph", "pub_year": "2021", "author_list": "Garza-L\u00f3pez, Roberto A.; Kozak, John J.; et el." }, { "id": "https://authors.library.caltech.edu/records/bda11-6nx75", "eprint_id": 104465, "eprint_status": "archive", "datestamp": "2023-08-22 05:40:28", "lastmod": "2024-01-17 17:27:02", "type": "monograph", "metadata_visibility": "show", "creators": { "items": [ { "id": "Kielb-Patrycja-J", "name": { "family": "Kielb", "given": "Patrycja J." }, "orcid": "0000-0003-2809-0813" }, { "id": "Gray-H-B", "name": { "family": "Gray", "given": "Harry B." }, "orcid": "0000-0002-7937-7876" }, { "id": "Winkler-Jay-R", "name": { "family": "Winkler", "given": "Jay R." }, "orcid": "0000-0002-4453-9716" } ] }, "title": "Does Tyrosine Protect S. Coelicolor Laccase from Oxidative Degradation?", "ispublished": "unpub", "full_text_status": "public", "keywords": "electron transfer; oxygen reduction; enzyme kinetics; tyrosyl radical; small laccase", "note": "Licence: CC BY-NC-ND 4.0. \n\nSubmitted date: 18/07/2020; Posted date: 20/07/2020. \n\nFunding: National Institute of Diabetes and Digestive and Kidney Diseases. \n\nAuthors declare no conflict of interest.\n\nSubmitted - Does_Tyrosine_Protect_S__Coelicolor_Laccase_from_Oxidative_Degradation__v1.pdf
", "abstract": "We have investigated the roles of tyrosine (Tyr) and tryptophan (Trp) residues in the four-electron reduction of oxygen catalyzed by Streptomyces coelicolor laccase (SLAC). During normal enzymatic turnover in laccases, reducing equivalents are delivered to a type 1 Cu center (Cu_(T1)) and then are transferred over 13 \u00c5 to a trinuclear Cu site (TNC: (Cu_(T3))\u2082Cu_(T2)) where O\u2082 reduction occurs. The TNC in SLAC is surrounded by a large cluster of Tyr and Trp residues that can provide reducing equivalents when the normal flow of electrons is disrupted. Canters and coworkers have shown that when O\u2082 reacts with a reduced SLAC variant lacking the CuT1 center, a Tyr108\u00b7 radical near the TNC forms rapidly. We have found that ascorbate reduces the Tyr108\u00b7 radical in wild-type SLAC about 10 times faster than it reacts with the Cu_(T1)\u00b2\u207a center, possibly owing to radical transfer along a Tyr/Trp chain. Aerobic oxidation of two reduced SLAC mutants (Y108F and W132F) leads to the formation of a long-lived (~15 min) Tyr\u00b7 radical with distinct absorption at 408 nm. The diffusion of redox equivalents away from the primary enzymatic pathway in SLAC may indicate a poorly optimized enzyme or a mechanism to protect against protein damage.", "date": "2020-07-21", "date_type": "published", "id_number": "CaltechAUTHORS:20200720-145555975", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20200720-145555975", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "National Institute of Diabetes and Digestive and Kidney Diseases" }, { "agency": "NIH" } ] }, "doi": "10.26434/chemrxiv.12671612", "primary_object": { "basename": "Does_Tyrosine_Protect_S__Coelicolor_Laccase_from_Oxidative_Degradation__v1.pdf", "url": "https://authors.library.caltech.edu/records/bda11-6nx75/files/Does_Tyrosine_Protect_S__Coelicolor_Laccase_from_Oxidative_Degradation__v1.pdf" }, "resource_type": "monograph", "pub_year": "2020", "author_list": "Kielb, Patrycja J.; Gray, Harry B.; et el." } ]