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Structural Basis of the Hydride Transfer Mechanism in F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase

MPG-Autoren
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Ceh,  Katharina
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Demmer,  Ulrike
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Warkentin,  Eberhard
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Moll,  Johanna
Max Planck Institute of Biophysics, Max Planck Society;

Thauer,  Rudolf K.
Max Planck Society;

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Shima,  Seigo
Max Planck Institute of Biophysics, Max Planck Society;

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Ceh, K., Demmer, U., Warkentin, E., Moll, J., Thauer, R. K., Shima, S., et al. (2009). Structural Basis of the Hydride Transfer Mechanism in F420-Dependent Methylenetetrahydromethanopterin Dehydrogenase. Biochemistry, 49(42), 10098-10105.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-D7C2-2
Zusammenfassung
F420-dependent methylenetetrahydromethanopterin (methylene-H4MPT) dehydrogenase (Mtd) of Methanopyrus kandleri is an enzyme of the methanogenic energy metabolism that catalyzes the reversible hydride transfer between methenyl-H4MPT+ and methylene-H4MPT using coenzyme F420 as hydride carrier. We determined the structures of the Mtd-methylene-H4MPT, Mtd-methenyl-H4MPT+, and the Mtd-methenyl- H4MPT+-F420H2 complexes at 2.1, 2.0, and 1.8 Å resolution, respectively. The pterin-imidazolidine-phenyl ring system is present in a new extended but not planar conformation which is virtually identical in methenyl- H4MPT+ andmethylene-H4MPT at the current resolution. Both substratesmethenyl-H4MPT+ and F420H2 bind in a face to face arrangement to an active site cleft, thereby ensuring a direct hydride transfer between their C14a andC5 atoms, respectively. The polypeptide scaffold does not reveal any significant conformational change upon binding of the bulky substrates but in turn changes the conformations of the substrate rings either to avoid clashes between certain ring atoms or to adjust the rings involved in hydride transfer for providing an optimal catalytic efficiency.