Browsing Kjemisk institutt by Author "Hersleth, Hans-Petter"
Now showing items 1-6 of 6
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Hammerstad, Marta; Kjendseth, Åsmund Røhr; Hersleth, Hans-Petter (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2019)Many laboratory courses consist of short and seemingly unconnected individual laboratory exercises. To increase the course consistency, relevance, and student engagement, we have developed a research‐inspired and project‐based ...
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Gudim, Ingvild; Hammerstad, Marta; Lofstad, Marie; Hersleth, Hans-Petter (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2018)Flavodoxins (Flds) are small, bacterial proteins that transfer electrons to various redox enzymes. Flavodoxins are reduced by ferredoxin/flavodoxin NADP+ oxidoreductases (FNRs), but little is known of the FNR-Fld interaction. ...
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Importance of Val567 on heme environment and substrate recognition of neuronal nitric oxide synthase Olsbu, Inger Kirstine; Zoppellaro, Giorgio; Andersson, Karl Kristoffer; Boucher, Jean-Luc; Hersleth, Hans-Petter (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2018)Nitric oxide (NO) produced by mammalian nitric oxide synthases (mNOSs) is an important mediator in a variety of physiological functions. Crystal structures of mNOSs have shown strong conservation of the active‐site residue ...
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Hammerstad, Marta; Hersleth, Hans-Petter (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2021)Structural studies show that enzymes have a limited number of unique folds, although structurally related enzymes have evolved to perform a large variety of functions. In this review, we have focused on enzymes containing ...
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Hammerstad, Marta; Gudim, Ingvild; Hersleth, Hans-Petter (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2020)Low G+C Gram-positive Firmicutes, such as the clinically important pathogens Staphylococcus aureus and Bacillus cereus, use the low-molecular weight thiol bacillithiol (BSH) as a defense mechanism to buffer the intracellular ...
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Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH-binding properties Shoor, Marita; Gudim, Ingvild; Hersleth, Hans-Petter; Hammerstad, Marta (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2021)Low molecular weight (low Mr) thioredoxin reductases (TrxRs) are homodimeric NADPH-dependent dithiol flavoenzymes that reduce thioredoxins (Trxs) or Trx-like proteins involved in the activation networks of enzymes, such ...