Stel een vraag
Met het formulier hier onder kunt u contact op nemen met boekwinkel Boekstra.
Bergner, Marie - Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands. Model Studies Using Synthetic Analogues - Model Studies Using Synthetic Analogues
De vraag gaat over de volgende titel:
Afbeelding: | |
---|---|
Schrijver: | Bergner, Marie |
Titel: | Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands. Model Studies Using Synthetic Analogues - Model Studies Using Synthetic Analogues |
ISBN: | 9783736996724 |
Uitgever: | Cuvillier Verlag |
Bijzonderheid: | 2017 198pp Paperback / softback |
Prijs: |
€ 52,00
Gratis
|
Meer info | Annotatie Iron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so called alternative ligands such as histidine have been recognized in Flaptekst Iron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so called alternative ligands such as histidine have been recognized in recent years. This work uses synthetic [2Fe-2S] analogues to explore the role alternative ligands play in determining the reactivity of iron sulfur clusters. Isomerization in a homoleptically coordinated cluster utilizing a mixed nitrogen- and sulfur-donating ligand is investigated as a model for ligand rearrangement processes during iron sulfur cluster biogenesis. Furthermore, a high fidelity model system for the asymmetrically ligated [2Fe-2S] cluster of mitoNEET proteins is developed and characterized in detail. This cluster and its homoleptic analogue are studied as reagents in proton coupled electron transfer processes, highlighting the role asymmetry and reorganization energy play in tuning this reactivity. The effects of the ligation pattern on entropic contributions during reduction are probed by temperature dependent electrochemical measurements. Finally, synthetic [2Fe-2S] clusters are investigated with respect to their reactivity with organic radicals, mimicking the unique reactivity of biotin synthase. |
Boek bekijken |
Verzendkosten 1,75 euro per zending binnen Nederland, vanaf 19,90 euro GEEN verzendkosten binnen Nederland.
Verzendkosten Belgiƫ 3,95 euro per zending.
Bij bestellingen van 10 euro of minder zijn de verzendkosten hoger; zie vermelding bij het boek.
Speciale verzoeken? Meestal geen punt, vermeld ze in het veld opmerking.
De actuele levertijd kunt u vinden op onze website.
De verkoper zal binnen 1 werkdag contact met u opnemen om de koop verder af te handelen.