Serial Femtosecond Zero Dose Crystallography Captures a Water-Free Distal Heme Site in a Dye-Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in Fe
X-ray serial femtosecond crystallography
arginine
bioinorganic
heme proteins
peroxidase
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
23 11 2020
23 11 2020
Historique:
received:
18
06
2020
pubmed:
12
8
2020
medline:
20
3
2021
entrez:
12
8
2020
Statut:
ppublish
Résumé
Obtaining structures of intact redox states of metal centers derived from zero dose X-ray crystallography can advance our mechanistic understanding of metalloenzymes. In dye-decolorising heme peroxidases (DyPs), controversy exists regarding the mechanistic role of the distal heme residues aspartate and arginine in the heterolysis of peroxide to form the catalytic intermediate compound I (Fe
Identifiants
pubmed: 32780931
doi: 10.1002/anie.202008622
pmc: PMC7756461
doi:
Substances chimiques
Coloring Agents
0
Iron Compounds
0
Heme
42VZT0U6YR
Arginine
94ZLA3W45F
Peroxidase
EC 1.11.1.7
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
21656-21662Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R021015/1
Pays : United Kingdom
Informations de copyright
© 2020 The Authors. Published by Wiley-VCH GmbH.
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