{"entity": "researcher", "timestamp": "2026-08-21T21:48:08.664Z", "family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "affiliations": ["Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden. hogbom@dbb.su.se."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/b427ce46a6ea4d908d67167e51d1b7d5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/b427ce46a6ea4d908d67167e51d1b7d5"}}, "publications": [{"entity": "publication", "iuid": "03b8b76f60b94595be68f854a95c97a9", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/03b8b76f60b94595be68f854a95c97a9.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/03b8b76f60b94595be68f854a95c97a9"}}, "title": "Author Correction: Characterization of a second class Ie ribonucleotide reductase.", "authors": [{"family": "John", "given": "Juliane", "initials": "J"}, {"family": "Lundin", "given": "Daniel", "initials": "D"}, {"family": "Branca", "given": "Rui M", "initials": "RM", "orcid": "0000-0003-3890-6476", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7f557cf4f7ed402c8843173ab0bbef04.json"}}, {"family": "Kumar", "given": "Rohit", "initials": "R", "orcid": "0000-0001-5033-2810", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fd150fa0a7254f878fb2ae6e564ba2e6.json"}}, {"family": "Srinivas", "given": "Vivek", "initials": "V", "orcid": "0000-0002-0265-1873", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5bbb4c7b9c734a87a398edc4e38cd97a.json"}}, {"family": "Lebrette", "given": "Hugo", "initials": "H", "orcid": "0000-0002-8081-181X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1df0bbc3d2f6465e8407bad4040b92b5.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b427ce46a6ea4d908d67167e51d1b7d5.json"}}], "type": "published erratum", "published": "2025-04-01", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "8", "issue": "1", "pages": "532", "issn-l": "2399-3642"}, "abstract": null, "doi": "10.1038/s42003-025-07982-4", "pmid": "40169876", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11961744"}, {"db": "pii", "key": "10.1038/s42003-025-07982-4"}], "notes": [], "created": "2026-08-20T09:25:26.677Z", "modified": "2026-08-20T09:25:26.759Z"}, {"entity": "publication", "iuid": "003e736990694b799b028ddf0f4379ec", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/003e736990694b799b028ddf0f4379ec.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/003e736990694b799b028ddf0f4379ec"}}, "title": "Characterization of a second class Ie ribonucleotide reductase.", "authors": [{"family": "John", "given": "Juliane", "initials": "J"}, {"family": "Lundin", "given": "Daniel", "initials": "D"}, {"family": "Branca", "given": "Rui M", "initials": "RM", "orcid": "0000-0003-3890-6476", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7f557cf4f7ed402c8843173ab0bbef04.json"}}, {"family": "Kumar", "given": "Rohit", "initials": "R", "orcid": "0000-0001-5033-2810", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fd150fa0a7254f878fb2ae6e564ba2e6.json"}}, {"family": "Srinivas", "given": "Vivek", "initials": "V", "orcid": "0000-0002-0265-1873", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5bbb4c7b9c734a87a398edc4e38cd97a.json"}}, {"family": "Lebrette", "given": "Hugo", "initials": "H", "orcid": "0000-0002-8081-181X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1df0bbc3d2f6465e8407bad4040b92b5.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b427ce46a6ea4d908d67167e51d1b7d5.json"}}], "type": "journal article", "published": "2025-02-22", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "8", "issue": "1", "pages": "281", "issn-l": "2399-3642"}, "abstract": "Class I ribonucleotide reductases (RNRs) convert ribonucleotides into deoxyribonucleotides under oxic conditions. The R2 subunit provides a radical required for catalysis conducted by the R1 subunit. In most R2s the radical is generated on a tyrosine via oxidation by an adjacent metal site. The discovery of a metal-free R2 defined the new RNR subclass Ie. In R2e, three of the otherwise strictly conserved metal-binding glutamates in the active site are substituted. Two variants have been found, VPK and QSK. To date, the VPK version has been the focus of biochemical characterization. Here we characterize a QSK variant of R2e. We analyse the organismal distribution of the two R2e versions and find dozens of organisms relying solely on the QSK RNR for deoxyribonucleotide production. We demonstrate that the R2eQSK of the human pathogen Gardnerella vaginalis (Bifidobacterium vaginale) modifies the active site-adjacent tyrosine to DOPA. The amount of modified protein is shown to be dependent on coexpression with the other proteins encoded in the RNR operon. The DOPA containing R2eQSK can support ribonucleotide reduction in vitro while the unmodified protein cannot. Finally, we determined the first structures of R2eQSK in the unmodified and DOPA states.", "doi": "10.1038/s42003-025-07565-3", "pmid": "39987380", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11846895"}, {"db": "pii", "key": "10.1038/s42003-025-07565-3"}], "notes": [], "created": "2026-08-20T09:25:22.863Z", "modified": "2026-08-20T09:25:23.134Z"}, {"entity": "publication", "iuid": "b1fe0adaedef4844a174a56d5ca2ee7d", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/b1fe0adaedef4844a174a56d5ca2ee7d.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/b1fe0adaedef4844a174a56d5ca2ee7d"}}, "title": "Metal-independent ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens", "authors": [{"family": "Srinivas", "given": "Vivek", "initials": "V"}, {"family": "Lebrette", "given": "Hugo", "initials": "H"}, {"family": "Lundin", "given": "Daniel", "initials": "D"}, {"family": "Kutin", "given": "Yuri", "initials": "Y"}, {"family": "Sahlin", "given": "Margareta", "initials": "M"}, {"family": "Lerche", "given": "Michael", "initials": "M"}, {"family": "Eirich", "given": "J\u00fcrgen", "initials": "J"}, {"family": "Branca", "given": "Rui M M", "initials": "RMM"}, {"family": "Cox", "given": "Nicholas", "initials": "N"}, {"family": "Sj\u00f6berg", "given": "Britt Marie", "initials": "BM"}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b427ce46a6ea4d908d67167e51d1b7d5.json"}}], "type": "posted-content", "published": "2018-06-15", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/348268", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:10:18.240Z", "modified": "2026-08-20T11:10:18.292Z"}, {"entity": "publication", "iuid": "64d4989610614c7da8c871413a79456d", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/64d4989610614c7da8c871413a79456d.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/64d4989610614c7da8c871413a79456d"}}, "title": "Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.", "authors": [{"family": "Griese", "given": "Julia J", "initials": "JJ", "orcid": "0000-0003-3686-3062", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/82045ff1a87e4f8997ef556daed43efa.json"}}, {"family": "Kositzki", "given": "Ramona", "initials": "R"}, {"family": "Schrapers", "given": "Peer", "initials": "P"}, {"family": "Branca", "given": "Rui M M", "initials": "RM", "orcid": "0000-0003-3890-6476", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7f557cf4f7ed402c8843173ab0bbef04.json"}}, {"family": "Nordstr\u00f6m", "given": "Anders", "initials": "A", "orcid": "0000-0003-3676-817X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bec4444d9bda475c87f2965d50021c9a.json"}}, {"family": "Lehti\u00f6", "given": "Janne", "initials": "J"}, {"family": "Haumann", "given": "Michael", "initials": "M"}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b427ce46a6ea4d908d67167e51d1b7d5.json"}}], "type": "journal article", "published": "2015-10-16", "journal": {"title": "J Biol Chem", "issn": "1083-351X", "volume": "290", "issue": "42", "pages": "25254-25272", "issn-l": "0021-9258"}, "abstract": "Two recently discovered groups of prokaryotic di-metal carboxylate proteins harbor a heterodinuclear Mn/Fe cofactor. These are the class Ic ribonucleotide reductase R2 proteins and a group of oxidases that are found predominantly in pathogens and extremophiles, called R2-like ligand-binding oxidases (R2lox). We have recently shown that the Mn/Fe cofactor of R2lox self-assembles from Mn(II) and Fe(II) in vitro and catalyzes formation of a tyrosine-valine ether cross-link in the protein scaffold (Griese, J. J., Roos, K., Cox, N., Shafaat, H. S., Branca, R. M., Lehti\u00f6, J., Gr\u00e4slund, A., Lubitz, W., Siegbahn, P. E., and H\u00f6gbom, M. (2013) Proc. Natl. Acad. Sci. U.S.A. 110, 17189-17194). Here, we present a detailed structural analysis of R2lox in the nonactivated, reduced, and oxidized resting Mn/Fe- and Fe/Fe-bound states, as well as the nonactivated Mn/Mn-bound state. X-ray crystallography and x-ray absorption spectroscopy demonstrate that the active site ligand configuration of R2lox is essentially the same regardless of cofactor composition. Both the Mn/Fe and the diiron cofactor activate oxygen and catalyze formation of the ether cross-link, whereas the dimanganese cluster does not. The structures delineate likely routes for gated oxygen and substrate access to the active site that are controlled by the redox state of the cofactor. These results suggest that oxygen activation proceeds via similar mechanisms at the Mn/Fe and Fe/Fe center and that R2lox proteins might utilize either cofactor in vivo based on metal availability.", "doi": "10.1074/jbc.M115.675223", "pmid": "26324712", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC4646176"}, {"db": "pii", "key": "S0021-9258(20)44547-8"}, {"db": "PDB", "key": "4HR0"}, {"db": "PDB", "key": "4HR4"}, {"db": "PDB", "key": "4XB9"}, {"db": "PDB", "key": "4XBV"}, {"db": "PDB", "key": "4XBW"}, {"db": "PDB", "key": "5DCO"}, {"db": "PDB", "key": "5DCR"}, {"db": "PDB", "key": "5DCS"}], "notes": [], "created": "2018-12-05T10:13:19.094Z", "modified": "2026-08-21T12:03:15.770Z"}]}