{"entity": "researcher", "timestamp": "2026-06-15T16:59:07.633Z", "family": "Molin", "given": "Mikael", "initials": "M", "orcid": "0000-0002-3903-8503", "affiliations": [], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/12e9dc11d1b047d88913ea3bcb2694be.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/12e9dc11d1b047d88913ea3bcb2694be"}}, "publications": [{"entity": "publication", "iuid": "430743aeba504beba191852cb4a81905", "links": {"self": {"href": "https://publications.scilifelab.se/publication/430743aeba504beba191852cb4a81905.json"}, "display": {"href": "https://publications.scilifelab.se/publication/430743aeba504beba191852cb4a81905"}}, "title": "Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.", "authors": [{"family": "Troussicot", "given": "Laura", "initials": "L", "orcid": "0000-0001-8297-8886", "researcher": {"href": "https://publications.scilifelab.se/researcher/e1f0d5dfcf0a4998a94ca70484e1a16a.json"}}, {"family": "Vallet", "given": "Alicia", "initials": "A"}, {"family": "Molin", "given": "Mikael", "initials": "M", "orcid": "0000-0002-3903-8503", "researcher": {"href": "https://publications.scilifelab.se/researcher/12e9dc11d1b047d88913ea3bcb2694be.json"}}, {"family": "Burmann", "given": "Bj\u00f6rn M", "initials": "BM", "orcid": "0000-0002-3135-7964", "researcher": {"href": "https://publications.scilifelab.se/researcher/b7a6d61fc1a64677874973c3247b1eb4.json"}}, {"family": "Schanda", "given": "Paul", "initials": "P", "orcid": "0000-0002-9350-7606", "researcher": {"href": "https://publications.scilifelab.se/researcher/fb928813cef545fdb7878b863ad096f9.json"}}], "type": "journal article", "published": "2023-05-17", "journal": {"title": "J. Am. Chem. Soc.", "issn": "1520-5126", "volume": "145", "issue": "19", "pages": "10700-10711", "issn-l": "0002-7863"}, "abstract": "Disulfide bond formation is fundamentally important for protein structure and constitutes a key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen peroxide through a catalytic cycle of Cys oxidation and reduction. Additionally, upon Cys oxidation PRDXs undergo extensive conformational rearrangements that may underlie their presently structurally poorly defined functions as molecular chaperones. Rearrangements include high molecular-weight oligomerization, the dynamics of which are, however, poorly understood, as is the impact of disulfide bond formation on these properties. Here we show that formation of disulfide bonds along the catalytic cycle induces extensive \u03bcs time scale dynamics, as monitored by magic-angle spinning NMR of the 216 kDa-large Tsa1 decameric assembly and solution-NMR of a designed dimeric mutant. We ascribe the conformational dynamics to structural frustration, resulting from conflicts between the disulfide-constrained reduction of mobility and the desire to fulfill other favorable contacts.", "doi": "10.1021/jacs.3c01200", "pmid": "37140345", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC10197130"}], "notes": [], "created": "2023-05-31T16:06:45.691Z", "modified": "2025-10-17T13:03:53.855Z"}, {"entity": "publication", "iuid": "e85aac1ccfe44c689708ad7b122acfa4", "links": {"self": {"href": "https://publications.scilifelab.se/publication/e85aac1ccfe44c689708ad7b122acfa4.json"}, "display": {"href": "https://publications.scilifelab.se/publication/e85aac1ccfe44c689708ad7b122acfa4"}}, "title": "Genetically controlled mtDNA deletions prevent ROS damage by arresting oxidative phosphorylation.", "authors": [{"family": "Stenberg", "given": "Simon", "initials": "S", "orcid": "0000-0003-0300-1730", "researcher": {"href": "https://publications.scilifelab.se/researcher/d59ba977fddf4071928bca5fdfc04ba2.json"}}, {"family": "Li", "given": "Jing", "initials": "J"}, {"family": "Gjuvsland", "given": "Arne B", "initials": "AB"}, {"family": "Persson", "given": "Karl", "initials": "K"}, {"family": "Demitz-Helin", "given": "Erik", "initials": "E"}, {"family": "Gonz\u00e1lez Pe\u00f1a", "given": "Carles", "initials": "C", "orcid": "0000-0002-7771-7988", "researcher": {"href": "https://publications.scilifelab.se/researcher/e92cd4ba564e4d0999681bf59cc95c70.json"}}, {"family": "Yue", "given": "Jia-Xing", "initials": "JX", "orcid": "0000-0002-2122-9221", "researcher": {"href": "https://publications.scilifelab.se/researcher/9c17dbcd3dff4f61aed7cc85a3a7136a.json"}}, {"family": "Gilchrist", "given": "Ciaran", "initials": "C"}, {"family": "\u00c4reng\u00e5rd", "given": "Timmy", "initials": "T"}, {"family": "Ghiaci", "given": "Payam", "initials": "P"}, {"family": "Larsson-Berglund", "given": "Lisa", "initials": "L"}, {"family": "Zackrisson", "given": "Martin", "initials": "M"}, {"family": "Smits", "given": "Silvana", "initials": "S"}, {"family": "Hallin", "given": "Johan", "initials": "J"}, {"family": "H\u00f6\u00f6g", "given": "Johanna L", "initials": "JL", "orcid": "0000-0003-2162-3816", "researcher": {"href": "https://publications.scilifelab.se/researcher/f1eaedff964f4060ae6e69f59cad4521.json"}}, {"family": "Molin", "given": "Mikael", "initials": "M", "orcid": "0000-0002-3903-8503", "researcher": {"href": "https://publications.scilifelab.se/researcher/12e9dc11d1b047d88913ea3bcb2694be.json"}}, {"family": "Liti", "given": "Gianni", "initials": "G", "orcid": "0000-0002-2318-0775", "researcher": {"href": "https://publications.scilifelab.se/researcher/96fb0b05418743bc9966610ff45a3220.json"}}, {"family": "Omholt", "given": "Stig W", "initials": "SW", "orcid": "0000-0002-8320-4337", "researcher": {"href": "https://publications.scilifelab.se/researcher/8a0f2458dfa64ac09c95356b1baf9f55.json"}}, {"family": "Warringer", "given": "Jonas", "initials": "J", "orcid": "0000-0001-6144-2740", "researcher": {"href": "https://publications.scilifelab.se/researcher/864cb0fde85a4aaeb68627f67e97d283.json"}}], "type": "journal article", "published": "2022-07-08", "journal": {"title": "Elife", "issn": "2050-084X", "volume": "11", "issn-l": "2050-084X"}, "abstract": "Deletion of mitochondrial DNA in eukaryotes is currently attributed to rare accidental events associated with mitochondrial replication or repair of double-strand breaks. We report the discovery that yeast cells arrest harmful intramitochondrial superoxide production by shutting down respiration through genetically controlled deletion of mitochondrial oxidative phosphorylation genes. We show that this process critically involves the antioxidant enzyme superoxide dismutase 2 and two-way mitochondrial-nuclear communication through Rtg2 and Rtg3. While mitochondrial DNA homeostasis is rapidly restored after cessation of a short-term superoxide stress, long-term stress causes maladaptive persistence of the deletion process, leading to complete annihilation of the cellular pool of intact mitochondrial genomes and irrevocable loss of respiratory ability. This shows that oxidative stress-induced mitochondrial impairment may be under strict regulatory control. If the results extend to human cells, the results may prove to be of etiological as well as therapeutic importance with regard to age-related mitochondrial impairment and disease.", "doi": "10.7554/eLife.76095", "pmid": "35801695", "labels": {"Integrated Microscopy Technologies Gothenburg": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC9427111"}, {"db": "pii", "key": "76095"}], "notes": [], "created": "2023-02-16T08:26:04.422Z", "modified": "2023-02-16T08:26:04.606Z"}, {"entity": "publication", "iuid": "70318c3b06a746719dc27afb6e0d57a1", "links": {"self": {"href": "https://publications.scilifelab.se/publication/70318c3b06a746719dc27afb6e0d57a1.json"}, "display": {"href": "https://publications.scilifelab.se/publication/70318c3b06a746719dc27afb6e0d57a1"}}, "title": "Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function.", "authors": [{"family": "Troussicot", "given": "Laura", "initials": "L", "orcid": "0000-0001-8297-8886", "researcher": {"href": "https://publications.scilifelab.se/researcher/e1f0d5dfcf0a4998a94ca70484e1a16a.json"}}, {"family": "Burmann", "given": "Bj\u00f6rn M", "initials": "BM", "orcid": "0000-0002-3135-7964", "researcher": {"href": "https://publications.scilifelab.se/researcher/b7a6d61fc1a64677874973c3247b1eb4.json"}}, {"family": "Molin", "given": "Mikael", "initials": "M", "orcid": "0000-0002-3903-8503", "researcher": {"href": "https://publications.scilifelab.se/researcher/12e9dc11d1b047d88913ea3bcb2694be.json"}}], "type": "journal article", "published": "2021-07-01", "journal": {"title": "Structure", "issn": "1878-4186", "volume": "29", "issue": "7", "pages": "640-654", "issn-l": "0969-2126"}, "abstract": "Peroxiredoxins (PRDXs) are abundant peroxidases present in all kingdoms of life. Recently, they have been shown to also carry out additional roles as molecular chaperones. To address this emerging supplementary function, this review focuses on structural studies of 2-Cys PRDX systems exhibiting chaperone activity. We provide a detailed understanding of the current knowledge of structural determinants underlying the chaperone function of PRDXs. Specifically, we describe the mechanisms which may modulate their quaternary structure to facilitate interactions with client proteins and how they are coordinated with the functions of other molecular chaperones. Following an overview of PRDX molecular architecture, we outline structural details of the presently best-characterized peroxiredoxins exhibiting chaperone function and highlight common denominators. Finally, we discuss the remarkable structural similarities between 2-Cys PRDXs, small HSPs, and J-domain-independent Hsp40 holdases in terms of their functions and dynamic equilibria between low- and high-molecular-weight oligomers.", "doi": "10.1016/j.str.2021.04.007", "pmid": "33945778", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pii", "key": "S0969-2126(21)00123-4"}], "notes": [], "created": "2021-07-02T14:04:18.036Z", "modified": "2025-10-17T13:03:55.754Z"}, {"entity": "publication", "iuid": "ce4c21c5846e448796cea17aa113b78f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/ce4c21c5846e448796cea17aa113b78f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/ce4c21c5846e448796cea17aa113b78f"}}, "title": "Light-sensing via hydrogen peroxide and a peroxiredoxin.", "authors": [{"family": "Bodvard", "given": "Kristofer", "initials": "K"}, {"family": "Peeters", "given": "Ken", "initials": "K"}, {"family": "Roger", "given": "Friederike", "initials": "F"}, {"family": "Romanov", "given": "Natalie", "initials": "N"}, {"family": "Igbaria", "given": "Aeid", "initials": "A"}, {"family": "Welkenhuysen", "given": "Niek", "initials": "N"}, {"family": "Palais", "given": "Ga\u00ebl", "initials": "G"}, {"family": "Reiter", "given": "Wolfgang", "initials": "W"}, {"family": "Toledano", "given": "Michel B", "initials": "MB"}, {"family": "K\u00e4ll", "given": "Mikael", "initials": "M"}, {"family": "Molin", "given": "Mikael", "initials": "M", "orcid": "0000-0002-3903-8503", "researcher": {"href": "https://publications.scilifelab.se/researcher/12e9dc11d1b047d88913ea3bcb2694be.json"}}], "type": "journal article", "published": "2017-03-24", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "8", "issue": "1", "pages": "14791", "issn-l": "2041-1723"}, "abstract": "Yeast lacks dedicated photoreceptors; however, blue light still causes pronounced oscillations of the transcription factor Msn2 into and out of the nucleus. Here we show that this poorly understood phenomenon is initiated by a peroxisomal oxidase, which converts light into a hydrogen peroxide (H 2O2) signal that is sensed by the peroxiredoxin Tsa1 and transduced to thioredoxin, to counteract PKA-dependent Msn2 phosphorylation. Upon H2O2, the nuclear retention of PKA catalytic subunits, which contributes to delayed Msn2 nuclear concentration, is antagonized in a Tsa1-dependent manner. Conversely, peroxiredoxin hyperoxidation interrupts the H2O2 signal and drives Msn2 oscillations by superimposing on PKA feedback regulation. Our data identify a mechanism by which light could be sensed in all cells lacking dedicated photoreceptors. In particular, the use of H2O2 as a second messenger in signalling is common to Msn2 oscillations and to light-induced entrainment of circadian rhythms and suggests conserved roles for peroxiredoxins in endogenous rhythms.", "doi": "10.1038/ncomms14791", "pmid": "28337980", "labels": {"Integrated Microscopy Technologies Gothenburg": "Service"}, "xrefs": [{"db": "pii", "key": "ncomms14791"}, {"db": "pmc", "key": "PMC5376668"}], "notes": [], "created": "2020-01-23T16:34:25.369Z", "modified": "2021-06-21T15:40:28.799Z"}]}