Differentiated Zn (II) binding affinities in animal, plant, and bacterial metallothioneins define their zinc buffering capacity at physiological pZn
K Mosna, K Jurczak, A Krężel - Metallomics, 2023 - academic.oup.com
Abstract Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
Phytochelatins Bind Zn (II) with Micro-to Picomolar Affinities without the Formation of Binuclear Complexes, Exhibiting Zinc Buffering and Muffling Rather than Storing …
M Łuczkowski, W Leszczyńska, J Wątły… - Inorganic …, 2024 - ACS Publications
Phytochelatins (PCs) are poly-Cys peptides containing a repeating γ-Glu-Cys motif
synthesized in plants, algae, certain fungi, and worms by PC synthase from reduced …
synthesized in plants, algae, certain fungi, and worms by PC synthase from reduced …
[PDF][PDF] Differentiated Zn (II) binding affinities in animal, plant, and
K Mosna, K Jurczak, A Krężel - 2023 - researchgate.net
Abstract Metallothioneins (MTs) are small, Cys-rich proteins present in various but not all
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …
organisms, from bacteria to humans. They participate in zinc and copper metabolism, toxic …