Gerhard Schenk

ORCID: 0000-0001-8619-0631
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About
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Research Areas
  • Metal complexes synthesis and properties
  • Crystallization and Solubility Studies
  • X-ray Diffraction in Crystallography
  • Metalloenzymes and iron-sulfur proteins
  • Antibiotic Resistance in Bacteria
  • Enzyme Catalysis and Immobilization
  • Metal-Catalyzed Oxygenation Mechanisms
  • Enzyme Structure and Function
  • Biochemical and Molecular Research
  • Enzyme Production and Characterization
  • Crystallography and molecular interactions
  • Photosynthetic Processes and Mechanisms
  • Microbial Metabolic Engineering and Bioproduction
  • Pesticide and Herbicide Environmental Studies
  • Tuberculosis Research and Epidemiology
  • Biofuel production and bioconversion
  • Pneumocystis jirovecii pneumonia detection and treatment
  • Magnetism in coordination complexes
  • Amino Acid Enzymes and Metabolism
  • Enzyme function and inhibition
  • Metabolism and Genetic Disorders
  • Phytase and its Applications
  • Peptidase Inhibition and Analysis
  • Trace Elements in Health
  • Antibiotics Pharmacokinetics and Efficacy

The University of Queensland
2016-2025

Queens University
2020

Sustainable Sciences Institute
2020

Brisbane School of Theology
2016-2020

Ecogenomics (Japan)
2019

National University of Ireland, Maynooth
2010-2013

Helwan University
2012

National University of Ireland
2011

Utah State University
2007-2010

Australian National University
2008-2010

Abstract Acetohydroxyacid synthase (AHAS) is the target for more than 50 commercial herbicides; first applied to crops in 1980s. Since then, 197 site-of-action resistance isolates have been identified weeds, with mutations at P197 and W574 most prevalent. Consequently, AHAS risk of not being a useful crop protection. To develop new herbicides, functional understanding explain effect these on activity required. Here, we show that can two effects (i) reduce binding affinity herbicides (ii)...

10.1038/s41467-022-31023-x article EN cc-by Nature Communications 2022-06-11

Ancestral sequence reconstruction is a technique that gaining widespread use in molecular evolution studies and protein engineering. Accurate requires the ability to handle appropriately large numbers of sequences, as well insertion deletion (indel) events, but available approaches exhibit limitations. To address these limitations, we developed Graphical Representation Sequence Predictions (GRASP), which efficiently implements maximum likelihood methods enable inference ancestors families...

10.1371/journal.pcbi.1010633 article EN cc-by PLoS Computational Biology 2022-10-24

Processive endoglucanase is a typical bifunctional biocatalyst for cellulose degradation. A GH5 processive from Bacillus subtilis BS-5 was previously identified and shown to exhibit highly efficient catalytic performance. To further augment its efficiency, both consensus mutagenesis loop engineering were applied. Compared the wild-type enzyme, variant (M3-1) with four point mutations, i.e., K91I, A198T, Q237D, V240P, exhibits an 8.5- 4.8-fold increase in efficiency toward soluble substrate...

10.1021/acscatal.4c01083 article EN ACS Catalysis 2024-04-18

Purple acid phosphatases (PAPs) are a family of binuclear metalloenzymes that catalyze the hydrolysis phosphoric esters and anhydrides. A PAP in sweet potato has unique, strongly antiferromagnetically coupled Fe(III)–Mn(II) center is distinguished from other PAPs by its increased catalytic efficiency for range activated unactivated phosphate esters, strict requirement Mn(II), presence μ-oxo bridge at pH 4.90. This enzyme displays maximum ( k cat / K m ) 4.5, whereas rate constant maximal...

10.1073/pnas.0407239102 article EN Proceedings of the National Academy of Sciences 2004-12-29

This communication reports the synthesis and X-ray structure of first mixed-valence FeIIIZnII complex containing FeIII(μ-OH)ZnII structural unit. Based on structure, physicochemical solution studies, catalytic properties toward hydrolysis diester 2,4-bis(dinitrophenyl)phosphate (BDNPP), it is proposed that 1 employs a hydrolytic mechanism similar to for red kidney bean purple acid phosphatase, including nucleophilic attack by terminal, FeIII-bound hydroxide concomitant release...

10.1021/ja071184l article EN Journal of the American Chemical Society 2007-05-23

To efficiently catalyze a chemical reaction, enzymes are required to maintain fast rates for formation of the Michaelis complex, reaction and product release. These distinct demands could be satisfied via fluctuation between different conformational substates (CSs) with unique configurations catalytic properties. However, there is debate as how these rapid changes, or dynamics, exactly affect catalysis. As model system, we have studied bacterial phosphotriesterase (PTE), which catalyzes...

10.1073/pnas.0907548106 article EN Proceedings of the National Academy of Sciences 2009-12-05

Abstract This microreview describes the structures and properties of a number bimetallic complexes designed as both structural functional mimics active sites some specific metallohydrolase enzymes. The metalloenzymes in question include predominantly monoesterase‐activity‐displaying purple acid phosphatase (PAP) di‐ triesterase enzymes, which have significant roles bioremedial hydrolysis organophosphate pesticides nerve gases. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2009)

10.1002/ejic.200900231 article EN European Journal of Inorganic Chemistry 2009-06-08

The bacterial phosphotriesterases catalyze hydrolysis of the pesticide paraoxon with very fast turnover rates and are thought to be near their evolutionary limit for this activity. To test whether naturally evolved rate could improved through incorporation unnatural amino acids probe role peripheral active site residues in nonchemical steps catalytic cycle (substrate binding product release), we replaced occurring tyrosine acid at position 309 L-(7-hydroxycoumarin-4-yl)ethylglycine (Hco)...

10.1021/ja106416g article EN Journal of the American Chemical Society 2010-12-16

Purple acid phosphatases (PAPs) are a group of metallohydrolases that contain dinuclear FeIIIMII center (MII = Fe, Mn, Zn) in the active site and able to catalyze hydrolysis variety phosphoric esters. The complex [(H2O)FeIII(μ-OH)ZnII(L-H)](ClO4)2 (2) with ligand 2-[N-bis(2-pyridylmethyl)aminomethyl]-4-methyl-6-[N′-(2-pyridylmethyl)(2-hydroxybenzyl) aminomethyl]phenol (H2L-H) has recently been prepared is found closely mimic coordination environment FeIIIZnII red kidney bean PAP (Neves et...

10.1021/ic101433t article EN Inorganic Chemistry 2010-11-16

Due to their aerobic lifestyle, eukaryotic organisms have evolved different strategies overcome oxidative stress. The recruitment of some specific metalloenzymes such as superoxide dismutases (SODs) and catalases (CATs) is great importance for eliminating harmful reactive oxygen species (hydrogen peroxide anion). Using the ligand HPClNOL {1-[bis(pyridin-2-ylmethyl)amino]-3-chloropropan-2-ol}, we synthesized three coordination compounds containing iron(III), copper(II), manganese(II) ions,...

10.1016/j.freeradbiomed.2014.12.005 article EN publisher-specific-oa Free Radical Biology and Medicine 2014-12-13

It is becoming increasingly apparent that the secondary coordination sphere can have a crucial role in determining functional properties of biomimetic metal complexes. We therefore designed and prepared variety ligands as metallo-hydrolase mimics, where hydrogen bonding second able to influence structure primary substrate binding. The assessment structure-function relationship based on derivates 2,6-bis{[bis(pyridin-2-ylmethyl)amino]methyl}-4-methylphenol (HBPMP = HL(1))...

10.1021/ic5009945 article EN Inorganic Chemistry 2014-08-14
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