bluuebunny/crossref_metadata_2025_split huggingface dataset:
Embracing Te Ao Māori to Rebuild a Sustainable Future for Chefs in Aotearoa New Zealand
Authors: Woodhouse Adrian , Humphreys Chloe 
Published: May 2024

The professional kitchen is a fast-paced environment often founded on hierarchical structures and stressful working conditions. Within this environment, tensions often run high resulting in aggressive behaviours, and at times, bullying and violence towards junior chefs. For the last decade the hospitality sector has been struggling to recruit and retain aspiring chefs into the professional kitchen. Compounding the recruitment issue is the social narrative that the hospitality industry is a poorly paid profession that works long and unsociable hours.
Due to the global pandemic the hospitality sector has suffered significant upheaval resulting in significant numbers of its workforce choosing to leave the industry. Like other countries around the globe, the hospitality sector in Aotearoa New Zealand is having to rethink and reset the way it operates in a new post covid landscape. Central to this is the questioning of established modes of practice and reimagining a new hospitality future.
In response to the changing landscape of hospitality, the Bachelor of Culinary Arts programme at Te Kura Matakini ki Otago (Otago Polytechnic), Aotearoa New Zealand developed a bicultural pedagogic framework that embraces te ao Māori values. As a strategy to educate chefs into alternative workplace behaviours and cultures the values of manaakitaka (care and integrity towards self and others), whānaukataka (integrity of relationship), and kotahitaka (a sense of collective unity and ownership) are deliberately integrated into the programmes pedagogy and the courses learning outcomes. In doing so, this pedagogic framework upholds the world views, values, and mana of Aotearoa’s takata whenua (Indigenous people), while also attempting to rebalance the historical practices of the professional kitchen.
Kolofon P20
Authors: Christoffersen Erik Exe 
Published: May 2024

Peripeti
© Peripeti og forfatterne
Temaredaktion

Nila Parly og Lars Ole Bonde.
Redaktion
Janicke Branth, Erik Exe Christoffersen (ansv.), Michael Eigtved, Solveig Gade, Louise Ejgod Hansen, Falk Heinrich, Birgitte Hesselaa, Kjersti Hustvedt, Thomas D. Kragebæk, Jens Christian Lauenstein Led, Thomas Rosendal Nielsen, Laura Luise Schultz, Kenn Lund Nielsen, Elin Andersen, Rasmus Malling Skov og Mads Thygesen.
Layout: Kenn Lund Nielsen
Omslagsfoto: The Picture o/Dorian Gray med Maximilian Schmid i hovedrollen. Den Jyske Opera. Foto Anders Bach.
Bagsidefoto: Falstajf med Donnie Ray Albert i hovedrollen. Det Kongelige Teater. Foto Miklos Szabo.

Tryk: Werks Offset
Oplag: 500
ISSN: 1604-0325
Peripeti udgives af Afdeling for Dramaturgi (Aarhus Universitet) i samarbejde med Teatervidenskah (Københavns Universitet) og Dramatikeruddannelsen (Aarhus Teater). Tidsskriftet udgives med støtte fra Forskningsrådet for Kultur og Kommunikation.
Alle temaartikler er fagfællevurderede.
Redaktionsadresse
Peripeti
Afdeling for Dramaturgi
Institut for Æstetik og Kommunikation, Aarhus Universitet,
Langelandsgade 139, DK- 8000 Århus C.
E-mail: aekexe@hum.au.dk www.peripeti.dk
Bestilling og abonnement peripeti@hum.au.dk Abonnement (to numre): 150 kr. Løssalg 100 kr.
Internet: http://www.peripeti.dk/bestilling/
Peripeti udkommer to gange om året.
Kolofon P25
Authors: Christoffersen Erik Exe 
Published: May 2024

Peripeti
© Peripeti og forfatterne

Temaredaktion
Erik Exe Christoffersen, Falk Heinrich og Laura Luise Schultz
Redaktion
Elin Andersen, Janicke Branth, Erik Exe Christoffersen (ansv.), Michael Eigtved, Solveig Gade, Falk Heinrich, Birgitte Hesselaa, Kjersti Hustvedt, Thomas D. Kragebæk, Jens Christian Lauenstein Led, Kenn Lund Nielsen, Thomas Rosendal Nielsen, Laura Luise Schultz, Rasmus Malling Skov og Mads Thygesen.
Layout: Kenn Lund Nielsen

Forside: La Monnaie de Munt I Hotel Pro Forma: Rachmaninov Troika IAleko Bagside: Rachmaninov Troika IFrancesca
Foto: Matthias og Clarchen Baus

Tryk: Werks Offset Oplag: 500
ISSN: 1604-0325
Peripeti udgives af Afdeling for Dramaturgi og Musikvidenskab (Aarhus Universitet), Af­ deling for Teater og-performancestudier (Københavns Universitet) og Dramatikeruddan­ nelsen (Den Danske Scenekunstskole). Tidsskriftet udgives med støtte fra Forskningsrådet for Kultur og Kommunikation.
Redaktionsadresse
Peripeti
Afdeling for Dramaturgi og Musikvidenskab Institut for Kommunikation og Kultur, Aarhus Universitet,
Langelandsgade 139, DK- 8000 Århus C.
E-mail: aekexe@cc.au.dk. Hjemmeside: www.peripeti.dk

Bestilling og abonnement
Abonnement (to numre): 150 kr. Løssalg 100 kr. Internet: http://www.peripeti.dk/bestilling/
Peripeti udkommer to gange om året
Phosphotriesterase
Authors: Bigley Andrew N , Raushel Frank M 
Published: September 2010

AbstractPhosphotriesterase (PTE) is a member of the amidohydrolase superfamily with the ability to hydrolyze numerous organophosphate substrates including many insecticides and nerve agents. The native active site metal is zinc, but the enzyme is fully active with a variety of metals. The overall fold of PTE is a (β/α)8TIM‐barrel with the active site located at the C‐terminal end of the barrel. The active site contains the binuclear metal center with the metal ligands being four histidines, an aspartate, and a carboxylated lysine from the C‐terminal ends of the β‐strands. In addition, the metal center contains a bridging hydroxyl that serves as the nucleophile in the SN2‐like reaction. The substrate‐binding site is external to the metal center and is made of residues from the loops connecting the C‐terminal end of each β‐strand to the subsequent α‐helix. The best known substrate for PTE is the insecticide paraoxon, which has a kinetic efficiency that approaches the limits of diffusion. PTE has significant potential as an enzyme tool for the detection and decontamination of pesticides and nerve agents. Numerous variants of PTE have been developed by directed evolution with improved kinetic efficiency toward various organophosphates.
Octaheme CytochromecNitrite Reductase
Authors: Tikhonova Tamara V , Polyakov Konstantin M , Boyko Konstantin M , Safonova Tatiana N , Popov Vladimir O 
Published: September 2010

AbstractOctaheme cytochromecnitrite reductase (TvNiR) from bacteriumThioalkalivibrio nitratireducenscatalyzes the six‐electron reduction of nitrite and two‐electron reduction of hydroxylamine to ammonium without release of any intermediates. TvNiR also catalyzes the six‐electron reduction of sulfite to sulfide. High‐resolution structures of the TvNiR apo‐form and its complexes with the substrates (nitrite and sulfite) and inhibitors (azide and phosphate) were obtained. The subunit of TvNiR consists of two domains. The N‐terminal domain has a unique fold and contains three hemes. The remaining five hemes are located in the catalytic C‐terminal domain, with the heme arrangement, including the catalytic heme, being identical to that found in pentaheme cytochromecnitrite reductases (ccNiRs). The catalytic machinery of TvNiR resembles that of ccNiRs. It comprises the lysine residue in the proximal position of the catalytic heme, the catalytic triad of tyrosine, histidine, and arginine on the distal side, channels for the substrate and product transport, and two conserved Ca2+‐binding sites. The complete set of eight hemes forms a spatial pattern characteristic of other structurally characterized octaheme cytochromes. In the crystalline state and in solution, TvNiR exists as a stable hexamer containing 48 hemes, which are clustered into three isolated groups, each group comprising 16 interacting hemes.
The Organomercurial LyaseMerB
Authors: Lello Paola Di , Lafrance‐Vanasse Julien , Omichinski James G 
Published: September 2010

AbstractMercury is introduced into the environment either from natural occurrences or from human activities, and consumption of mercury‐contaminated fish poses a serious human health issue. The three inorganic forms of mercury are elemental mercury, mercurous compounds, and mercuric compounds, while the most abundant organic form is methylmercury. Owing to its ability to permeate membranes and accumulate in organisms, methylmercury is more toxic than ionic mercury. Mercury‐resistant bacteria have developed a two enzyme system to convert both Hg (II) and methylmercury to the less toxic elemental mercury. The first enzyme is an organomercurial lyase (MerB) and the second enzyme is a mercuric ion reductase (MerA). MerB catalyzes the protonolysis of the carbon–mercury bond on a wide range of organomercurials, including methylmercury, resulting in a reduced carbon compound and ionic mercury. The cleavage of the carbon–mercury bond and the formation of the electrophile‐carbon bond are concerted (SE2). Structural studies demonstrated that MerB contains a unique fold and that significant conformational changes occur on binding of organomercurial substrates. On the basis of mutagenesis, structural, and computational studies, two cysteines and an aspartic acid residue in the active site are known to play key roles in the cleavage of the carbon–mercury bond.
Two‐Domain Multicopper Oxidase
Authors: Lawton Thomas J , Rosenzweig Amy C 
Published: September 2010

AbstractTwo‐domain multicopper oxidases (2dMCOs) couple the four‐electron reduction of dioxygen to the oxidation of a number of different substrates, including organic compounds and reduced ferricytochromes. The geometry of 2dMCO active sites is similar to that in other multicopper oxidases, but is formed by a significantly different protein architecture. This fold resembles the overall architecture of NO forming copper nitrite reductase (CuNIR). 2dMCOs are classified based on the location of their type‐1 copper centers.
3‐Ketosteroid‐9α‐Hydroxylase
Authors: Capyk Jenna K , Strynadka Natalie C , Eltis Lindsay D 
Published: September 2010

AbstractKshAB is a Rieske oxygenase (RO) in the aerobic steroid degradation pathways of bacteria. It is a monooxygenase responsible for the 9α‐hydroxylation of the nucleus of 3‐keto‐4‐ene steroids bearing short side chains at C17. It is composed of two domains arranged in a head‐to‐tail fashion to form the functional trimer. The N‐terminal Rieske domain harbors a Fe2S2cluster in which the two irons are coordinated by two cysteine and two histidine residues, respectively. The larger, C‐terminal catalytic domain contains a mononuclear nonheme iron coordinated by a His‐His‐Asp facial triad. Purified KshAB fromMycobacterium tuberculosisexhibits substrate specificities for 1,4‐androstadien‐3,17‐one and dioxygen 2‐3 orders of magnitude lower than those measured for other ROs and their best substrates. In agreement with the large fused‐ring substrate, the structure of KshA incorporates an active site channel and substrate binding pocket that are longer than those observed in other ROs, and positioned in a different relative orientation within the catalytic domain. KshA also possesses a C‐terminal helix which occupies a position not observed in other RO structures and which likely stabilizes trimeric quaternary structure. Finally, KshA exhibits a minimal core catalytic domain with respect to secondary structural elements that may prove archetypical for ROs.
Toluene 4‐Monooxygenase and its Complex with Effector ProteinT4moD
Authors: Bailey Lucas J , Fox Brian G 
Published: September 2010

AbstractToluene 4‐monooxygenase (T4MO) is a multiprotein diiron enzyme complex that catalyzes the regiospecific oxidation of toluene top‐cresol. Catalytic function requires the presence of a small protein, called theeffector protein. Effector protein exerts substantial control on the diiron hydroxylase catalytic cycle through protein–protein interactions. High‐resolution crystal structures of the stoichometric hydroxylase and effector protein complex described here reveal how protein–protein interactions and reduction of the diiron center produce an active site configuration poised for reaction with O2. Further information from crystal structures of mutated isoforms of the hydroxylase and a peroxo adduct is combined with catalytic results to give a fuller picture of the geometry of the enzyme–substrate complex used for the high fidelity oxidation of hydrocarbon substrates.
Zinc TransporterYiiPfromEscherichia coli
Authors: Fu Dax 
Published: September 2010

AbstractYiiP fromEscherichia colibelongs to the protein family of cation diffusion facilitator (CDF). CDFs play critical roles in metal homeostatic controls in microbes, plants, and mammals. They utilize the proton motive force to drive effluxes of transition metal ions out of the cytoplasm. Bacterial CDFs primarily contribute to metal resistance while mammalian CDFs are more involved in metal metabolism and cellular signaling. The crystal structure of YiiP reveals a Y‐shaped dimeric architecture, consisting of a transmembrane domain and a cytoplasmic domain that adopts a metallochaperone‐like fold. The molecular details of three distinct zinc coordination sites in YiiP delineate how metallochemistry is tailored to three central functions of CDFs: selective metal binding, rapid transport kinetics, and allosteric regulation of the transport activity. An integration of the structural information and existing biochemical data allows us to propose a two‐modular model for the operation of YiiP. In this model, the transmembrane domain is responsible for a stoichiometric zinc‐for‐proton exchange across the membrane barrier. The cytoplasmic domain detects the fluctuation of zinc concentrations and responds with a conformational change that is transmitted to regulate the activity of the transmembrane domain. In addition, the cytoplasmic domain may also serve as a zinc receiving module for uploading of the zinc cargo from a putative zinc‐metallochaperone.
X‐Ray Crystallography
Authors: Guss Jules Mitchell 
Published: September 2010

AbstractX‐ray crystallography is the most extensively practised and widely applicable technique for determining molecular structures. These may be relatively small coordination complexes or metalloproteins with masses exceeding 1000 kda. The accuracy of the structures may range from a few thousands of Ǻngstrom for a small molecules to a few tenths of an Ǻngstrom for a protein. The major limitation of the technique is the requirement for well‐diffracting crystals.
Alkylation—Chemistry and Fundamentals
Authors: Albright Lyle F. 
Published: September 2010

AbstractAlkylation of isobutane and aromatics have been performed commercially using liquid catalysts for many years to produce the following: high quality gasolines and alkyl benzenes (including ethyl benzene, cumene, and intermediates for detergents). Liquid–liquid dispersions or liquid–gas systems are used which contain protonic acids or Friedel–Crafts compounds as catalysts. The chemistry, which is always complicated, is reviewed to explain formation of the main products and by‐products. Different catalysts often result in significantly different chemistry. Fewer details are available on the following: relative kinetics of competing and simultaneous reactions plus physical phenomena affecting the overall processes. The ionic reactions generally occur at or near the interfacial areas between phases (often the catalyst and hydrocarbon phases). Mass transfer steps are often, if not always, of major importance. Recent information on the physical steps is discussed.
Alkylation—Industrial
Authors: Albright Lyle F. 
Published: September 2010

AbstractCommercial processes to alkylate isobutane and aromatics are described and evaluated. Liquid catalysts are used for alkylations of isobutane to produce high quality gasolines. For this alkylation, solid catalysts have been widely investigated, but none has yet been commercialized. Liquid catalysts were once used exclusively for alkylation of aromatics to produce a variety of petrochemicals, but solid catalysts are now widely used. Methods on how to improve these various processes are recommended.
Ammonia Synthesis—Biological
Authors: Newton William E. 
Published: September 2010

AbstractDinitrogen (N2) in the earth's atmosphere cannot be metabolized directly by most organisms and, consequently, cellular nitrogen is usually obtained as an already reactive form, such as ammonia or nitrate. These sources of “fixed” nitrogen are relatively scarce and most often limit agricultural production. Because organic nitrogen is incompletely recycled and because available ammonia and nitrate are continually metabolized to N2, the biological reduction of N2occupies a pivotal position in the biogeochemical nitrogen cycle. This process, called nitrogen fixation, is performed only by prokaryotic microorganisms and catalyzed by the enzyme, nitrogenase. N2‐fixing microorganisms may be either free‐living or associated symbiotically with other microbes, plants, or infrequently animals. The most agriculturally significant are the symbiotic microorganisms that live within plant tissues. The most common nitrogenase is the molybdenum‐(Mo)based enzyme, but similar vanadium‐based and iron‐based enzymes are known plus a fourth unique system. The structure of its two component proteins and their 2:1 complex are known. Most nitrogenases catalyze the reduction of other substrates, such as C2H2and HCN, in reactions inhibited by CO. Substrate reduction involves association–dissociation cycles in which electrons (accompanied by MgATP hydrolysis) are transferred between component proteins. Each nitrogenase is genetically distinct, and its biosynthesis, maturation, and activity are regulated by the products of up to 19 genes. A fundamental understanding of the biochemical action and genetic regulation of the nitrogen‐fixation components has significant potential for improving the economy of nitrogen fixation, minimizing water pollution, and increasing global food supplies.
Carbonylation—Heterogeneous
Authors: Stepanov Alexander G. 
Published: September 2010

AbstractIn this article basic heterogeneous carbonylation catalysts known to date and their application for the conversion of the particular olefins, alcohols, alkanes into carboxylic acids, ketones, aldehydes etc., have been described. Two approaches for the design of heterogeneous catalysts are considered. The first one is a direct heterogenization of high efficiency homogeneous carbonylation catalysts used in the Reppe reaction. This approach is based on the three ways of heterogenization of homogeneous metal complexes: By anchoring on polymers, amorphous oxides or zeolites, and inert carbonaceous supports. These metal‐ or metal‐complex‐supported catalysts usually require alkyl halide promoters. The other approach consists of using the analogues of the liquid strong‐acid catalysts in the Koch reaction, that is, the pure solid acidic catalysts, such as acidic zeolites, heteropoly acids, acidic ion‐exchanged resins, and sulfated zirconia. Analysis of the carbonylation catalysts is given on the basis of the type of support used in the first approach, the required promotor, and the conditions for carbonylation performance (liquid phase or vapor‐phase carbonylation) in both approaches.
Catalyst Preparation—Homogeneous
Authors: Keep Ann 
Published: September 2010

AbstractThe preparation of homogeneous catalysts is discussed. Particular emphasis is given to the preparation of platinum group metal catalysts. The issues of whether to use a catalyst or catalyst precursor, that is a preformed orin situcatalyst, the catalyst oxidation state, ligand attachment, and ligand synthesis are discussed. In addition, patent issues and environmental issues are raised. The incorporation of cocatalysts and additives is discussed, and stability and handling issues are considered. Sometimes homogeneous catalysts are in fact used as precursors to nanoparticles or colloids. Some examples of homogeneous catalyst preparation are given; there are Ziegler catalysts for alkene hydrogenation, base metal catalysts such as bis(1,5‐cyclooctadiene) nickel(0) for the oligomerization of acetylene and the dimerization of dienes, (R,R)‐(–)‐(1,2‐cyclohexanediamino‐N,N′‐bis(3,5‐di‐t‐butylsalicylidene))manganese(III) chloride, Jacobsen's epoxidation catalyst, (2,6‐diisopropylphenylimido)(neophylidene)bis(hexafluoro‐tert‐butoxide)molybdenum(VI), and Schrock's alkene metathesis catalyst. Preparations of platinum group metal catalysts such as tris(triphenylphosphine)chlororhodium(I) (Wilkinson's catalyst) for hydrogenations, palladium tetrakis(triphenylphosphine) for carbon–carbon coupling reactions and iridium(cyclooctadiene)chloride dimer, a precursor for hydrogenations and hydrosilylations are also given.
Chiral Catalysts
Authors: Kégl Tamás , Kollár László 
Published: September 2010

AbstractThe application of optically active compounds is steadily increasing due to their biological importance. The most efficient way for their synthesis is catalysis, i.e., a reaction where a small amount of chiral material (catalyst) can transmit chirality to a large amount of substrate. Of the various types of chiral catalysts, the present article is dealing exclusively with those containing transition metals in liquid phase.In the first part of the article the chiral ligands are arranged according to their donor atoms, and classified as phosphanes (mono‐ and bidentate phosphanes possessing various elements of chirality), nitrogen, and oxygen ligands, etc. This section is followed by chiral catalysts grouped systematically according to their central metal. (The discussion is restricted to those homogeneous chiral catalysts, where the chemical transformation of an achiral substrate possessing enantiotopic groups, atoms, faces, or centers into one enantiomer takes place.) While in the “ligand section,” the seminal works on the synthesis of the most widely used basic ligands and their first applications are demonstrated, in the “metal section,” the most recent applications (over the past 5 years) are discussed.
Chiral Catalysts
Authors: Kégl Tamás , Kollár László 
Published: September 2010

AbstractThe application of optically active compounds is steadily increasing due to their biological importance. The most efficient way for their synthesis is catalysis, that is a reaction where a small amount of chiral material (catalyst) can transmit chirality to a large amount of substrate.Of the various types of chiral catalysts, the present article deals exclusively with those containing transition metals in the liquid phase.In the first part of the article, the chiral ligands are arranged according to their donor atoms and are classified as phosphanes (mono‐ and bidentate phosphanes, possessing various elements of chirality), nitrogen and oxygen ligands, chiral dienes, etc. This section is followed by chiral catalysts grouped systematically according to their central metal. (The discussion is restricted to those homogeneous chiral catalysts, where the chemical transformation of an achiral substrate possessing enantiotopic groups, atoms, faces, or centers into one enantiomer takes place.) While the section dealing with ligand, the seminal works on the synthesis of the most widely used basic ligands and their first applications are also demonstrated and in the section dealing with metal mainly the recent catalytic (synthetic) applications over the past 10 years are discussed.
Copper Enzymes/Models
Authors: Park Ga Young , Lee Dong‐Heon , Karlin Kenneth D. 
Published: September 2010

Abstract

Copper is utilized as a catalytic metal center in a variety of enzymes involved in oxidation–reduction processes. The Cu(I) and Cu(II) oxidation states are readily accessible and interconvertible under physiological conditions via oxidants (ie, O
2
) or reducing agents such as ascorbic acid or glutathione. The important chemical transformations that these enzymes are responsible for include dioxygen processing as well as nitrogen oxide (NOx) conversions. The active site structures and catalytic mechanisms of the most well‐studied copper enzymes are described. The contributions to the understanding of enzyme function obtained from biomimetic studies using synthetic copper complexes of most relevance to the active site features have also been highlighted.