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Britt-Marie Sjöberg

Britt-Marie Sjöberg

D-Index & Metrics

Chemistry

D-Index
64
Citations
11531
World Ranking
8211
National Ranking
108

Biology and Biochemistry

D-Index
66
Citations
12221
World Ranking
8872
National Ranking
116

Research.com Recognitions

  • 2017 - Member of Academia Europaea

Overview

Britt-Marie Sjöberg is a researcher affiliated with Stockholm University in Sweden. Their work primarily spans the fields of Biochemistry, Genetics and Molecular Biology, as well as Chemistry. Within these domains, their research focuses on several subfields including Molecular Biology, Inorganic Chemistry, Materials Chemistry, Renewable Energy, Sustainability and the Environment, and Genetics.

The scientist's research topics cover a range of specialized subjects, notably Metal-Catalyzed Oxygenation Mechanisms, ATP Synthase and ATPases Research, Enzyme Structure and Function, RNA and protein synthesis mechanisms, Bacterial Genetics and Biotechnology, Advanced Electron Microscopy Techniques and Applications, and Antimicrobial Resistance in Staphylococcus.

Among the recent papers authored or coauthored by Sjöberg are:

  • A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases, 2022, Nature Communications
  • A ribonucleotide reductase from Clostridium botulinum reveals distinct evolutionary pathways to regulation via the overall activity site, 2020, Journal of Biological Chemistry
  • Structure of a ribonucleotide reductase R2 protein radical, 2023, Science
  • Radical Enzymes, 2020, Encyclopedia of Life Sciences
  • Structural and Biochemical Investigation of Class I Ribonucleotide Reductase from the Hyperthermophile Aquifex aeolicus, 2021, Biochemistry

Sjöberg has published frequently in venues such as bioRxiv (Cold Spring Harbor Laboratory), eLife, Nature Communications, Science, and the Journal of Biological Chemistry. Their publication record shows multiple contributions to these respected platforms, with three papers in bioRxiv and two in eLife.

The scientist collaborates with several frequent co-authors, including Inna Rozman Grinberg, Daniel Lundin, Derek T. Logan, Ipsita A. Banerjee, and Ornella Bimaï. These collaborations reflect a substantial collaborative network within their research community.

In recognition of contributions to their field, Sjöberg was awarded membership in the Academia Europaea in 2017.

Best Publications

  • Three-dimensional structure of the free radical protein of ribonucleotide reductase

    Pär Nordlund;Britt-Marie Sjöberg;Hans Eklund

  • Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.

    Mathias Eriksson;Ulla Uhlin;S Ramaswamy;Monica Ekberg

  • DNA building blocks: keeping control of manufacture.

    Anders Hofer;Mikael Crona;Derek T. Logan;Britt-Marie Sjöberg

  • The iron center in ribonucleotide reductase from Escherichia coli.

    L. Petersson;A. Gräslund;A. Ehrenberg;B.M. Sjöberg

  • Identification of the stable free radical tyrosine residue in ribonucleotide reductase.

    A Larsson;B M Sjöberg

  • The tyrosine free radical in ribonucleotide reductase from Escherichia coli.

    B M Sjöberg;P Reichard;A Gräslund;A Ehrenberg

  • A Glycyl Radical Site in the Crystal Structure of a Class III Ribonucleotide Reductase

    Derek T. Logan;Jessica Andersson;Britt-Marie Sjöberg;Pär Nordlund

  • Conformational and functional similarities between glutaredoxin and thioredoxins.

    H. Eklund;C. Cambillau;B.M. Sjöberg;A. Holmgren

  • Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism

    B. M. Sjöberg

  • Nature of the free radical in ribonucleotide reductase from Escherichia coli.

    B M Sjöberg;P Reichard

  • Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction.

    Climent I;Sjöberg Bm;Huang Cy

  • Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli

    Anders Åberg;Solveig Hahne;Margareta Karlsson;Åke Larsson

  • Two Conserved Tyrosine Residues in Protein R1 Participate in an Intermolecular Electron Transfer in Ribonucleotide Reductase

    Monica Ekberg;Margareta Sahlin;Mathias Eriksson;Britt-Marie Sjöberg

  • Magnetic interaction between the tyrosyl free radical and the antiferromagnetically coupled iron center in ribonucleotide reductase.

    Margareta Sahlin;Leif Petersson;Astrid Graeslund;Anders Ehrenberg

  • The Free Radical of the Anaerobic Ribonucleotide Reductase from Escherichia coli Is at Glycine 681

    Xueyin Sun;Sandrine Ollagnier;Peter P. Schmidt;Mohamed Atta

  • Raman spectral evidence for a mu-oxo bridge in the binuclear iron center of ribonucleotide reductase.

    B M Sjöberg;T M Loehr;J Sanders-Loehr

  • Electron Magnetic Resonance of the Tyrosyl Radical in Ribonucleotide Reductase from Escherichia coli

    Curtis W. Hoganson;Margareta Sahlin;§ and Britt-Marie Sjöberg;Gerald T. Babcock

  • The Crystal Structure of an Azide Complex of the Diferrous R2 Subunit of Ribonucleotide Reductase Displays a Novel Carboxylate Shift with Important Mechanistic Implications for Diiron-Catalyzed Oxygen Activation

    Martin E. Andersson;Martin Högbom;Agnes Rinaldo-Matthis;K. Kristoffer Andersson

  • A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene.

    Xueyin Sun;Jens Harder;Maria Krook;Hans Jornvall

  • A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2'-azido-2'-deoxynucleoside diphosphates.

    B M Sjöberg;A Gräslund;F Eckstein

Frequent Co-Authors

Astrid Gräslund
Astrid Gräslund Stockholm University
Pär Nordlund
Pär Nordlund Karolinska Institute
Hans Eklund
Hans Eklund Swedish University of Agricultural Sciences
Hans Jörnvall
Hans Jörnvall Karolinska Institute
Arne Holmgren
Arne Holmgren Karolinska Institute
Peter Reichard
Peter Reichard University of Padua
Wolfgang Lubitz
Wolfgang Lubitz Max Planck Society
Friedhelm Lendzian
Friedhelm Lendzian Technical University of Berlin
Marc Fontecave
Marc Fontecave Collège de France
Franck Fieschi
Franck Fieschi Grenoble Alpes University

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