Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase

Hinderberger, Dariush, Ebner, Sieglinde, Mayr, Stefan, Jaun, Bernhard, Reiher, Markus, Goenrich, Meike, Thauer, Rudolf K. and Harmer, Jeffrey (2008) Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase. Journal of Biological Inorganic Chemistry, 13 8: 1275-1289. doi:10.1007/s00775-008-0417-0


Author Hinderberger, Dariush
Ebner, Sieglinde
Mayr, Stefan
Jaun, Bernhard
Reiher, Markus
Goenrich, Meike
Thauer, Rudolf K.
Harmer, Jeffrey
Title Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase
Journal name Journal of Biological Inorganic Chemistry   Check publisher's open access policy
ISSN 0949-8257
1432-1327
Publication date 2008-11-01
Sub-type Article (original research)
DOI 10.1007/s00775-008-0417-0
Volume 13
Issue 8
Start page 1275
End page 1289
Total pages 15
Place of publication Heidelberg, Germany
Publisher Springer
Language eng
Formatted abstract
Methane formation in methanogenic Archaea is catalyzed by methyl-coenzyme M reductase (MCR) and takes place via the reduction of methyl-coenzyme M (CH3-S-CoM) with coenzyme B (HS-CoB) to methane and the heterodisulfide CoM-S–S-CoB. MCR harbors the nickel porphyrinoid coenzyme F430 as a prosthetic group, which has to be in the Ni(I) oxidation state for the enzyme to be active. To date no intermediates in the catalytic cycle of MCRred1 (red for reduced Ni) have been identified. Here, we report a detailed characterization of MCRred1m (“m” for methyl-coenzyme M), which is the complex of MCRred1a (“a” for absence of substrate) with CH3-S-CoM. Using continuous-wave and pulse electron paramagnetic resonance spectroscopy in combination with selective isotope labeling (13C and 2H) of CH3-S-CoM, it is shown that CH3-S-CoM binds in the active site of MCR such that its thioether sulfur is weakly coordinated to the Ni(I) of F430. The complex is stable until the addition of the second substrate, HS-CoB. Results from EPR spectroscopy, along with quantum mechanical calculations, are used to characterize the electronic and geometric structure of this complex, which can be regarded as the first intermediate in the catalytic mechanism.
Keyword Methyl-coenzyme M reductase
McR
Nickel enzyme
Catalytic cycle
Factor F(430)
Electron-Paramagnetic-Resonance
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Centre for Advanced Imaging Publications
 
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