Multimodal Response to Copper Binding in Superoxide Dismutase Dynamics.
Amyotrophic Lateral Sclerosis
/ metabolism
Binding Sites
Copper
/ chemistry
Crystallization
Histidine
/ chemistry
Humans
Kinetics
Magnetic Fields
Magnetic Resonance Spectroscopy
Metalloproteins
/ chemistry
Models, Molecular
Protein Conformation
Protein Multimerization
Superoxide Dismutase
/ chemistry
Zinc
/ chemistry
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
18 11 2020
18 11 2020
Historique:
pubmed:
10
11
2020
medline:
21
4
2021
entrez:
9
11
2020
Statut:
ppublish
Résumé
Copper/zinc superoxide dismutase (SOD) is a homodimeric metalloenzyme that has been extensively studied as a benchmark for structure-function relationships in proteins, in particular because of its implication in the familial form of the neurodegenerative disease amyotrophic lateral sclerosis. Here, we investigate microcrystalline preparations of two differently metalated forms of SOD, namely, the fully mature functional Cu,Zn state and the E,Zn-SOD state in which the Cu site is empty. By using solid-state NMR with fast magic-angle spinning (MAS) at high magnetic fields (
Identifiants
pubmed: 33166153
doi: 10.1021/jacs.0c09242
doi:
Substances chimiques
Metalloproteins
0
Histidine
4QD397987E
Copper
789U1901C5
Superoxide Dismutase
EC 1.15.1.1
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM