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  How [Fe]-Hydrogenase from Methanothermobacter is Protected Against Light and Oxidative Stress

Wagner, T., Huang, G., Ermler, U., & Shima, S. (2018). How [Fe]-Hydrogenase from Methanothermobacter is Protected Against Light and Oxidative Stress. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 57(46), 15056-15059. doi:10.1002/anie.201807203.

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Wagner, T.1, Author           
Huang, G.1, Author           
Ermler, U., Author
Shima, S.1, Author           
Affiliations:
1Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, Karl-von-Frisch-Strasse 10, D-35043 Marburg, DE, ou_3266277              

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 Abstract: [Fe]-hydrogenase (Hmd) catalyzes the reversible hydrogenation of methenyltetrahydromethanopterin (methenyl-H4 MPT+ ) with H2 . Hmd contains the iron-guanylylpyridinol (FeGP) cofactor, which is sensitive to light and oxidative stress. A natural protection mechanism is reported for Hmd based on structural and biophysical data. Hmd from Methanothermobacter marburgensis (mHmd) was found in a hexameric state, where an expanded oligomerization loop is detached from the dimer core and intrudes into the active site of a neighboring dimer. An aspartic acid residue from the loop ligates to FeII of the FeGP cofactor and thus blocks the postulated H2 -binding site. In solution, this enzyme is in a hexamer-to-dimer equilibrium. Lower enzyme concentrations, and the presence of methenyl-H4 MPT+ , shift the equilibrium toward the active dimer side. At higher enzyme concentrations-as present in the cell-the enzyme is predominantly in the inactive hexameric state and is thereby protected against light and oxidative stress.

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 Dates: 2018-11-12
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: eDoc: 747944
ISI: 000452396800010
DOI: 10.1002/anie.201807203
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Title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Source Genre: Journal
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Pages: - Volume / Issue: 57 (46) Sequence Number: - Start / End Page: 15056 - 15059 Identifier: ISSN: 1433-7851