Radical S-adenosylmethionine maquette chemistry: Cx
Cysteine motifs
Electron paramagnetic resonance spectroscopy
Ferredoxin
Iron sulfur clusters
Protoenzymes
Radical S-adenosylmethionine
UV–Vis spectroscopy
[4Fe–4S]-maquettes
Journal
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
ISSN: 1432-1327
Titre abrégé: J Biol Inorg Chem
Pays: Germany
ID NLM: 9616326
Informations de publication
Date de publication:
09 2019
09 2019
Historique:
received:
15
07
2019
accepted:
14
08
2019
pubmed:
6
9
2019
medline:
14
7
2020
entrez:
6
9
2019
Statut:
ppublish
Résumé
The synthesis and characterization of short peptide-based maquettes of metalloprotein active sites facilitate an inquiry into their structure/function relationships and evolution. The [4Fe-4S]-maquettes of bacterial ferredoxin metalloproteins (Fd) have been used in the past to engineer redox active centers into artificial metalloenzymes. The novelty of our study is the application of maquettes to the superfamily of [4Fe-4S] cluster and S-adenosylmethionine-dependent radical metalloenzymes (radical SAM). The radical SAM superfamily enzymes contain site-differentiated, redox active [4Fe-4S] clusters coordinated to Cx
Identifiants
pubmed: 31486952
doi: 10.1007/s00775-019-01708-8
pii: 10.1007/s00775-019-01708-8
doi:
Substances chimiques
C-Peptide
0
Ferredoxins
0
Iron-Sulfur Proteins
0
S-Adenosylmethionine
7LP2MPO46S
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
793-807Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM054608
Pays : United States
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