EPR spectroscopic characterisation of native Cu<sup>II</sup>-binding sites in human serum albumin-Reference-Cited by-同舟云学术

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EPR spectroscopic characterisation of native Cu^II-binding sites in human serum albumin

Published:2024 Issue:32 Volume:53 Page:13529-13536
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Ackermann Katrin¹^ORCID,Wu Dongmei²,Stewart Alan J.²^ORCID,Bode Bela E.¹^ORCID

Affiliation:

1. EaStCHEM School of Chemistry, Biomedical Sciences Research Complex, and Centre of Magnetic Resonance, University of St Andrews, St Andrews, KY16 9ST, UK

2. School of Medicine, Biomedical Sciences Research Complex, and Centre of Magnetic Resonance, University of St Andrews, St Andrews, KY16 9TF, UK

Abstract

Using a suite of electron paramagnetic resonance spectroscopy techniques to investigate single-histidine knockout mutants of human serum albumin, a set of three histidine residues can be determined as primary and secondary copper ion binding sites.

Funder

Wellcome Trust

Engineering and Physical Sciences Research Council

British Heart Foundation

Biotechnology and Biological Sciences Research Council

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/DT/D4DT00892H

Reference46 articles.

1. Structural and biochemical characterisation of Co²⁺-binding sites on serum albumins and their interplay with fatty acids

2. T.Peters , in All About Albumin , ed. T. Peters , Academic Press , San Diego , 1995 , pp. 76–132 , 10.1016/B978-012552110-9/50005-2

3. Binding of transition metal ions to albumin: Sites, affinities and rates

4. Albumin research in the 21st century

5. Albumin-mediated extracellular zinc speciation drives cellular zinc uptake

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