XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase.
Methanogens
Nickel
Serial femtosecond crystallography (SFX)
X-ray Diffraction (XRD)
X-ray Emission Spectroscopy (XES)
X-ray Free-Electron Laser (XFEL)
Journal
Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
received:
10
11
2021
revised:
10
02
2022
accepted:
10
02
2022
pubmed:
25
2
2022
medline:
6
5
2022
entrez:
24
2
2022
Statut:
ppublish
Résumé
Methyl-Coenzyme M Reductase (MCR) catalyzes the biosynthesis of methane in methanogenic archaea, using a catalytic Ni-centered Cofactor F430 in its active site. It also catalyzes the reverse reaction, that is, the anaerobic activation and oxidation, including the cleavage of the CH bond in methane. Because methanogenesis is the major source of methane on earth, understanding the reaction mechanism of this enzyme can have massive implications in global energy balances. While recent publications have proposed a radical-based catalytic mechanism as well as novel sulfonate-based binding modes of MCR for its native substrates, the structure of the active state of MCR, as well as a complete characterization of the reaction, remain elusive. Previous attempts to structurally characterize the active MCR-Ni(I) state have been unsuccessful due to oxidation of the redox- sensitive catalytic Ni center. Further, while many cryo structures of the inactive Ni(II)-enzyme in various substrates-bound forms have been published, no room temperature structures have been reported, and the structure and mechanism of MCR under physiologically relevant conditions is not known. In this study, we report the first room temperature structure of the MCRred1-silent Ni(II) form using an X-ray Free-Electron Laser (XFEL), with simultaneous X-ray Emission Spectroscopy (XES) and X-ray Diffraction (XRD) data collection. In celebration of the seminal contributions of inorganic chemist Dick Holm to our understanding of nickel-based catalysis, we are honored to announce our findings in this special issue dedicated to this remarkable pioneer of bioinorganic chemistry.
Identifiants
pubmed: 35202981
pii: S0162-0134(22)00057-5
doi: 10.1016/j.jinorgbio.2022.111768
pmc: PMC8930625
mid: NIHMS1783308
pii:
doi:
Substances chimiques
Oxidoreductases
EC 1.-
methyl coenzyme M reductase
EC 2.8.4.1
Methane
OP0UW79H66
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
111768Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM126289
Pays : United States
Organisme : NIGMS NIH HHS
ID : R56 GM055302
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM126982
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM110501
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM117126
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM055302
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM124169
Pays : United States
Organisme : NIH HHS
ID : S10 OD023453
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM139687
Pays : United States
Organisme : NIGMS NIH HHS
ID : P01 GM063210
Pays : United States
Informations de copyright
Copyright © 2022 Elsevier Inc. All rights reserved.
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