English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structure–Spectroscopy Correlations for Intermediate Q of Soluble Methane Monooxygenase: Insights from QM/MM Calculations

Schulz, C. E., Castillo, R. G., Pantazis, D. A., DeBeer, S., & Neese, F. (2021). Structure–Spectroscopy Correlations for Intermediate Q of Soluble Methane Monooxygenase: Insights from QM/MM Calculations. Journal of the American Chemical Society, 143(17), 6560-6577. doi:10.1021/jacs.1c01180.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
ja1c01180_si_001-1.pdf (Supplementary material), 9MB
Name:
ja1c01180_si_001-1.pdf
Description:
Supporting Information
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Schulz, Christine E.1, Author           
Castillo, Rebeca G.2, Author
Pantazis, Dimitrios A.1, Author           
DeBeer, Serena2, Author           
Neese, Frank3, Author           
Affiliations:
1Research Group Pantazis, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_2541711              
2Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023871              
3Research Department Neese, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_2541710              

Content

show
hide
Free keywords: -
 Abstract: The determination of the diiron core intermediate structures involved in the catalytic cycle of soluble methane monooxygenase (sMMO), the enzyme that selectively catalyzes the conversion of methane to methanol, has been a subject of intense interest within the bioinorganic scientific community. Particularly, the specific geometry and electronic structure of the intermediate that precedes methane binding, known as intermediate Q (or MMOHQ), has been debated for over 30 years. Some reported studies support a bis-μ-oxo-bridged Fe(IV)2O2 closed-core conformation Fe(IV)2O2 core, whereas others favor an open-core geometry, with a longer Fe–Fe distance. The lack of consensus calls for a thorough re-examination and reinterpretation of the spectroscopic data available on the MMOHQ intermediate. Herein, we report extensive simulations based on a hybrid quantum mechanics/molecular mechanics approach (QM/MM) approach that takes into account the complete enzyme to explore possible conformations for intermediates MMOHox and MMOHQ of the sMMOH catalytic cycle. High-level quantum chemical approaches are used to correlate specific structural motifs with geometric parameters for comparison with crystallographic and EXAFS data, as well as with spectroscopic data from Mössbauer spectroscopy, Fe K-edge high-energy resolution X-ray absorption spectroscopy (HERFD XAS), and resonance Raman 16O–18O difference spectroscopy. The results provide strong support for an open-core-type configuration in MMOHQ, with the most likely topology involving mono-oxo-bridged Fe ions and alternate terminal Fe-oxo and Fe-hydroxo groups that interact via intramolecular hydrogen bonding. The implications of an open-core intermediate Q on the reaction mechanism of sMMO are discussed.

Details

show
hide
Language(s): eng - English
 Dates: 2021-01-312021-04-222021-05-05
 Publication Status: Published in print
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.1c01180
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of the American Chemical Society
  Other : JACS
  Abbreviation : J. Am. Chem. Soc.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 143 (17) Sequence Number: - Start / End Page: 6560 - 6577 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870