Background and Aims: Patients undergoing surgery are prone to infections, either at the site of surgery (superficial or organ-space) or at remote sites (e.g. pneumonia or urinary tract). Surgical site infections are associated with substantial morbidity and mortality, increased length of hospital stay and represent a huge burden to the health economy across all healthcare systems. Here we discuss

All you need to know about @LiesLahousse, first ECM to be granted the Early Career Member Award; #LSC2020; the newly elected assembly representatives for @EarlyCareerERS; and new @EuroRespSoc fellowship opportunities http://bit.ly/2OTgQlo

The nature of today’s business demands that Business Analytics (BA) extends to an operational level to better support employees in their decision-making. This is noticeable from the constant requests for new reports and changes in old ones at different employee levels. As a result, BA specialists or other power-users in functional departments are “bombarded” by these requests, and it becomes more

In the mid-2000s, Danish and Norwegian criminal procedural law underwent legislative amendments to strengthen the rights of complainants in cases of sexual violence and other cases of serious violations. While in Norway complainants were afforded participatory rights and stronger legal representation in court, this was largely not the case in Denmark. The aim of this chapter is to identify how the

The sayings of the Desert Fathers had an important role in the monastic education and were very widespread. Originally written down in Greek, they were soon translated into all the main languages in the medieval Europe, and underwent transformations as they were copied. The sayings were organized in different ways, mainly alphabetically or according to themes, and as they were copied the repertoir

In his history of Swedish poets who wrote in (Humanist) Greek (1785–9), Matthias Floderus claimed that before his time such a mania for versification raged in the Swedish universities in Uppsala, Turku, Tartu, and Lund that hardly one academic specimen appeared without it being embellished with Greek verses by students – also prose texts occur. That claim is only slightly exaggerated. This paper p

Enzymes of the xanthine oxidase family are among the best characterized mononuclear molybdenum enzymes. Open questions about their mechanism of transfer of an oxygen atom to the substrate remain. The enzymes share a molybdenum cofactor (Moco) with the metal ion binding a molybdopterin (MPT) molecule via its dithiolene function and terminal sulfur and oxygen groups. For xanthine dehydrogenase (XDH)

The xanthine oxidase (XO) family comprises molybdenum-dependent enzymes that usually form homodimers (or dimers of heterodimers/trimers) organized in three domains that harbor two [2Fe-2S] clusters, one FAD, and a Mo cofactor. In this work, we crystallized an unusual member of the family, the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli. This is the first example of an E. coli

The class of [NiFe]-hydrogenases comprises oxygen-sensitive periplasmic (PH) and oxygen-tolerant membrane-bound (MBH) enzymes. For three PHs and four MBHs from six bacterial species, structural features of the nickel-iron active site of hydrogen turnover and of the iron-sulfur clusters functioning in electron transfer were determined using X-ray absorption spectroscopy (XAS). Fe-XAS indicated surp

[FeFe]-hydrogenase from green algae (HydA1) is the most efficient hydrogen (H2) producing enzyme in nature and of prime interest for (bio)technology. Its active site is a unique six-iron center (H-cluster) composed of a cubane cluster, [4Fe4S]H, cysteine-linked to a diiron unit, [2Fe]H, which carries unusual carbon monoxide (CO) and cyanide ligands and a bridging azadithiolate group. We have probe

The [FeFe]-hydrogenase (HydA1) from green algae is the minimal enzyme for efficient biological hydrogen (H2) production. Its active-site six-iron center (H-cluster) consists of a cubane, [4Fe4S]H, cysteine-linked to a diiron site, [2Fe]H. We utilized the spin-polarization of the iron Kβ X-ray fluorescence emission to perform site-selective X-ray absorption experiments for spectral discrimination o

Sulfite oxidase (SO) is an essential molybdoenzyme for humans, catalyzing the final step in the degradation of sulfur-containing amino acids and lipids, which is the oxidation of sulfite to sulfate. The catalytic site of SO consists of a molybdenum ion bound to the dithiolene sulfurs of one molybdopterin (MPT) molecule, carrying two oxygen ligands, and is further coordinated by the thiol sulfur of

The molybdenum cofactor is an important cofactor, and its biosynthesis is essential for many organisms, including humans. Its basic form comprises a single molybdopterin (MPT) unit, which binds a molybdenum ion bearing three oxygen ligands via a dithiolene function, thus forming Mo-MPT. In bacteria, this form is modified to form the bis-MPT guanine dinucleotide cofactor with two MPT units coordina

Two crystallized [FeFe] hydrogenase model complexes, 1 = (μ-pdt)[Fe(CO)2(PMe3)]2 (pdt = SC1H 2C2H2C3H2S), and their bridging-hydride (Hy) derivative, [1Hy]+ = [(μ-H)(μ-pdt)[Fe(CO)2 (PMe 3)]2]+ (BF4-), were studied by Fe K-edge X-ray absorption and emission spectroscopy, supported by density functional theory. Structural changes in [1Hy]+ compared to 1 involved small bond elongations (