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771.
Andrea Bombana Dr. Muralidharan Shanmugam Prof. David Collison Dr. Alexander J. Kibler Dr. Graham N. Newton Dr. Christof M. Jäger Prof. Anna K. Croft Dr. Simone Morra Dr. Nicholas J. Mitchell 《Chembiochem : a European journal of chemical biology》2023,24(18):e202300250
‘Bacterial-type’ ferredoxins host a cubane [4Fe4S]2+/+ cluster that enables these proteins to mediate electron transfer and facilitate a broad range of biological processes. Peptide maquettes based on the conserved cluster-forming motif have previously been reported and used to model the ferredoxins. Herein we explore the integration of a [4Fe4S]-peptide maquette into a H2-powered electron transport chain. While routinely formed under anaerobic conditions, we illustrate by electron paramagnetic resonance (EPR) analysis that these maquettes can be reconstituted under aerobic conditions by using photoactivated NADH to reduce the cluster at 240 K. Attempts to tune the redox properties of the iron-sulfur cluster by introducing an Fe-coordinating selenocysteine residue were also explored. To demonstrate the integration of these artificial metalloproteins into a semi-synthetic electron transport chain, we utilize a ferredoxin-inspired [4Fe4S]-peptide maquette as the redox partner in the hydrogenase-mediated oxidation of H2. 相似文献
772.
Ellen M. Fay Ailish Newton Dr. Mark Berney Dr. Afaf H. El-Sagheer Prof. Tom Brown Prof. Joanna F. McGouran 《Chembiochem : a European journal of chemical biology》2023,24(13):e202200756
We report a two-step validation approach to evaluate the suitability of metal-binding groups for targeting DNA damage-repair metalloenzymes using model enzyme SNM1A. A fragment-based screening approach was first used to identify metal-binding fragments suitable for targeting the enzyme. Effective fragments were then incorporated into oligonucleotides using the copper-catalysed azide–alkyne cycloaddition reaction. These modified oligonucleotides were recognised by SNM1A at >1000-fold lower concentrations than their fragment counterparts. The exonuclease SNM1A is a key enzyme involved in the repair of interstrand crosslinks, a highly cytotoxic form of DNA damage. However, SNM1A and other enzymes of this class are poorly understood, as there is a lack of tools available to facilitate their study. Our novel approach of incorporating functional fragments into oligonucleotides is broadly applicable to generating modified oligonucleotide structures with high affinity for DNA damage-repair enzymes. 相似文献
773.
do Carmo Devaney Ribeiro Peixoto Murilo Santos dos Santos Felipe Alexsandro Sales Abner Santos Baroni Filho Newton Luiz Dias de Souza Magossi Mariana 《SILICON》2023,15(2):683-697
Silicon - A zinc-modified octa(aminopropyl)silsesquioxane and the cyan compound Na2[Fe(CN)5NO] were prepared to create a hybrid electroactive material (ACZnN) characterized employing the... 相似文献