ingvigud

• Gudim, Ingvild; Hammerstad, Marta; Lofstad, Marie & Hersleth, Hans-Petter (2018). Characterization of different flavodoxin reductase-flavodoxin (FNR-Fld) interactions reveals an efficient FNR-Fld redox pair and identifies a novel FNR subclass. Biochemistry.  ISSN 0006-2960.  57(37), s 5427- 5436 . doi: 10.1021/acs.biochem.8b00674 Full text in Research Archive.
• Gudim, Ingvild; Lofstad, Marie; Van Beek, Wouter & Hersleth, Hans-Petter (2018). High-resolution crystal structures reveal a mixture of conformers of the Gly61-Asp62 peptide bond in an oxidized flavodoxin from Bacillus cereus. Protein Science.  ISSN 0961-8368.  27(8), s 1439- 1449 . doi: 10.1002/pro.3436
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta & Hersleth, Hans-Petter (2017). Measurement of FNR-NrdI Interaction by Microscale Thermophoresis (MST). Bio-protocol.  ISSN 2331-8325.  7(8), s e2223 . doi: 10.21769/BioProtoc.2223 Full text in Research Archive.
• Lofstad, Marie; Gudim, Ingvild; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2016). Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus. Biochemistry.  ISSN 0006-2960.  55(36), s 4998- 5001 . doi: 10.1021/acs.biochem.6b00699
• Ash, Philip A; Liu, Juan; Coutard, Nathan; Heidary, Nina; Horch, Marius; Gudim, Ingvild; Simler, Thomas; Zebger, Ingo; Lenz, Oliver & Vincent, Kylie A (2015). Electrochemical and Infrared Spectroscopic Studies Provide Insight into Reactions of the NiFe Regulatory Hydrogenase from Ralstonia eutropha with O2 and CO. Journal of Physical Chemistry B.  ISSN 1520-6106.  119, s 13807- 13815 . doi: 10.1021/acs.jpcb.5b04164

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• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Røhr, Åsmund Kjendseth & Hersleth, Hans-Petter (2019). Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; van Beek, Wouter & Hersleth, Hans-Petter (2019). New structural insight into the well known peptide flip observed in flavodoxins.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; van Beek, Wouter & Hersleth, Hans-Petter (2019). New structural insight into the well known peptide flip observed in flavodoxins. Acta Crystallographica Section A: Foundations and Advances.  ISSN 2053-2733.  A75, s e123- e123 . doi: 10.1107/S2053273319094336
• Hammerstad, Marta; Gudim, Ingvild; Lofstad, Marie; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2019). Characterization of Proteins in the Ribonucleotide Reductase RedoxNetwork.
• Hammerstad, Marta; Gudim, Ingvild; Lofstad, Marie; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2019). Enzyme activation by a flavoprotein redox network. Acta Crystallographica Section A: Foundations and Advances.  ISSN 2053-2733.  A75, s e128- e128 . doi: 10.1107/S2053273319094282
• Hammerstad, Marta; Gudim, Ingvild; Lofstad, Marie; Røhr, Åsmund Kjendseth & Hersleth, Hans-Petter (2019). Enzyme Activation by a Flavoprotein Redox Network.
• Gudim, Ingvild; Hersleth, Hans-Petter; Hammerstad, Marta & Sørlie, Morten (2018). Characterisation of flavodoxin and ferredoxin/flavodoxin reductases from Bacillus cereus and their interactions. Series of dissertations submitted to the Faculty of Mathematics and Natural Sciences, University of Oslo.. 2000.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta & Hersleth, Hans-Petter (2018). Enzyme activation by a flavoprotein redox network. NBS-nytt.  ISSN 0801-3535.  s 40- 40
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta & Hersleth, Hans-Petter (2018). Enzyme activation by a flavoprotein redox network.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Røhr, Åsmund Kjendseth & Hersleth, Hans-Petter (2018). Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta & Hersleth, Hans-Petter (2017). Enzyme activation by a flavoprotein redox network.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2017). Activation of the Class Ib Ribonucleotide Reductase by a Flavin Network in Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2017). Activation of the Class Ib Ribonucleotide Reductase by a Flavin Network in Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2017). Activation of the class IB ribonucleotide reductase by a flavodoxin reductase in Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2017). Activation of the class Ib RNR by a flavodoxin reductase in B. cereus. NSB-nytt.  s 105- 105
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2017). Activation of the class Ib ribonucleotide reductase by a flavodoxin reductase in Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2017). Activation of the class Ib ribonucleotide reductase by a flavodoxin reductase in Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2017). Activation of the class Ib ribonucleotide reductase by a flavodoxin reductase in Bacillus cereus.
• Lofstad, Marie; Gudim, Ingvild; Kjendseth, Åsmund Røhr; Andersen, Niels Højmark; van Beek, Wouter; Andersson, K. Kristoffer & Hersleth, Hans-Petter (2017). Combining Protein X-ray crystallography and in situ single-crystal UV-Vis and Raman spectroscopy to grasph the true structure of haem- and flavoproteins.
• Shoor, Marita; Gudim, Ingvild; Hammerstad, Marta & Hersleth, Hans-Petter (2017). Structural and functional characterization of redox proteins in an enzyme activating network involving the thioredoxin reductase in Bacillus cereus.
• Shoor, Marita; Hersleth, Hans-Petter; Gudim, Ingvild & Hammerstad, Marta (2017). Structural and functional characterization of the redox protein Thioredoxin reductase from Bacillus cereus.
• Gudim, Ingvild; Lofstad, Marie; Andersson, K. Kristoffer; Hammerstad, Marta & Hersleth, Hans-Petter (2016). Probing enzyme activation networks ‐ structural and functional studies of flavoproteins in Bacillus cereus. NBS-nytt.  ISSN 0801-3535.  s 45- 45
• Gudim, Ingvild; Lofstad, Marie; Hammerstad, Marta; Kjendseth, Åsmund Røhr & Hersleth, Hans-Petter (2016). Activation of the Class Ib Ribonucleotide Reductase by a Flavodoxin Reductase in Bacillus cereus.
• Hersleth, Hans-Petter; Gudim, Ingvild; Lofstad, Marie; Kjendseth, Åsmund Røhr; Van beek, Wouter; Giullaume, Pompidor; Mehmet, Can; Xiangbo, Zhao; Magliozzo, Richard s.; Bren, Kara L & Andersson, K. Kristoffer (2016). Grasping the True Structure of Haem- and Flavoproteins – Combining X-RAY Crystallography and In Situ Single-Crystal UV-VIS and Raman Spectroscopy.
• Lofstad, Marie; Gudim, Ingvild; Kjendseth, Åsmund Røhr; Hammerstad, Marta; Andersson, K. Kristoffer & Hersleth, Hans-Petter (2016). Activation of Class Ib Ribonucleotide Reductase by NRDI and Its Reductase Partner in Bacillus cereus.
• Lofstad, Marie; Gudim, Ingvild; Van beek, Wouter; Pompidor, Guillaume; Kjendseth, Åsmund Røhr; Andersson, K. Kristoffer & Hersleth, Hans-Petter (2016). Radiation damage of haem- and flavoproteins – combining X-ray crystallography and single-crystal UV-Vis and Raman spectroscopy.
• Lofstad, Marie; Gudim, Ingvild; Van beek, Wouter; Pompidor, Guillaume; Kjendseth, Åsmund Røhr; Andersson, K. Kristoffer & Hersleth, Hans-Petter (2016). Radiation damage of haem- and flavoproteins –combining X-ray crystallography and single-crystal UV-Vis and Raman spectroscopy. 9th International Workshop on X-ray Radiation Damage to Biological Crystalline Samples.
• Gudim, Ingvild (2015). Probing enyzme activation - a beginner's view on MST as a tool for biophysical studies.
• Gudim, Ingvild & Hersleth, Hans-Petter (2015). Structure of a ferredoxin/flavodoxin-NADP(H) oxidoreductase in Bacillus cereus.. NBS-nytt.  ISSN 0801-3535.  s 96- 96
• Gudim, Ingvild & Hersleth, Hans-Petter (2015). Structure of a ferredoxin/flavodoxin-NADP(H) oxidoreductase in Bacillus cereus..
• Gudim, Ingvild & Hersleth, Hans-Petter (2015). Structures of ferredoxin/flavodoxin-NADP(H) oxidoreductases in Bacillus cereus.
• Gudim, Ingvild & Hersleth, Hans-Petter (2015). Structures of ferredoxin/flavodoxin-NADP(H) oxidoreductases in Bacillus cereus.. Acta Crystallographica Section A: Foundations of Crystallography.  ISSN 0108-7673.  A71, s s205- s205 . doi: 10.1107/S2053273315096916
• Lofstad, Marie; Gudim, Ingvild; Skråmo, Silje; Hammerstad, Marta; Røhr, Åsmund Kjendseth; Tomter, Ane Berg; Andersson, K. Kristoffer & Hersleth, Hans-Petter (2014). Crystallisation of ferredoxin/flavodoxin-NADP(H) oxidoreductases, flavodoxins, ferredoxins and redox partners in Bacillus cereus. Show summary

  Crystallisation of ferredoxin/flavodoxin-NADP(H) oxidoreductases, flavodoxins, ferredoxins and redox partners in Bacillus cereus Lofstad M1, Gudim I1, Skråmo S1, Hammerstad, M1, Røhr ÅK1, Tomter AB1, Andersson KK1, Hersleth H-P1 1Depatment of Biosciences, Section for Biochemistry and Molecular Biology, University of Oslo, Oslo, Norway Ferredoxin/flavodoxin-NADP(H) oxidoreductases (FNRs) catalyses the reversible redox reaction between ferredoxins (Fds) or flavodoxins (Flds) and NAD(P)+/NAD(P)H. In oxygenic photosynthetic organisms FNRs catalyse the reduction of NADP+ by photosynthetically reduced Fd, while in many heterotrophs, FNRs catalyse the NADPH-dependent reduction of Fd/Fld to provide subsequently reducing power to different Fd/Fld-dependent enzyme systems. In Bacillus cereus there are three annotated FNRs that can be redox partners for three Flds and two Fds. We have without tags purified and crystallised several of these redox proteins in Bacillus cereus, and some of their redox partners. A goal of the project is to understand the recognition, selectivity and flexibility of these FNRs, Flds and Fds with respect to each other and their redox partners. References Skråmo S, et al., Acta Cryst. F70, 777-780 (2014) Hammerstad M, et al., ACS Chem. Biol. 9, 526-537 (2014) Røhr ÅK, et al., Angew. Chem. Int. Ed. 49, 2324-2327 (2010)

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