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Structure of a Quinohemoprotein Amine Dehydrogenase with an Uncommon Redox Cofactor and Highly Unusual Crosslinking

Datta, Saumen ; Mori, Youichi ; Takagi, Kazuyoshi ; Kawaguchi, Katsunori ; Chen, Zhi-Wei ; Okajima, Toshihide ; Kuroda, Shun'ichi ; Ikeda, Tokuji ; Kano, Kenji ; Tanizawa, Katsuyuki ; Mathews, F. Scott

Proceedings of the National Academy of Sciences - PNAS, 2001-12, Vol.98 (25), p.14268-14273 [Periódico revisado por pares]

United States: National Academy of Sciences

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Título:
Structure of a Quinohemoprotein Amine Dehydrogenase with an Uncommon Redox Cofactor and Highly Unusual Crosslinking
Autor: Datta, Saumen ; Mori, Youichi ; Takagi, Kazuyoshi ; Kawaguchi, Katsunori ; Chen, Zhi-Wei ; Okajima, Toshihide ; Kuroda, Shun'ichi ; Ikeda, Tokuji ; Kano, Kenji ; Tanizawa, Katsuyuki ; Mathews, F. Scott
Assuntos: Active sites ; Amines ; Amino Acid Sequence ; Amino acids ; Atoms ; Biochemistry ; Biological Sciences ; Catalytic Domain ; Coenzymes - biosynthesis ; Coenzymes - chemistry ; Cross-Linking Reagents ; Crystallography, X-Ray ; cysteine tryptophylquinone ; cytochrome c ; Cytochromes ; Dehydrogenases ; Enzymes ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Open reading frames ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors - biosynthesis ; Oxidoreductases Acting on CH-NH Group Donors - chemistry ; Oxidoreductases Acting on CH-NH Group Donors - genetics ; Oxygen ; Paracoccus denitrificans ; Paracoccus denitrificans - enzymology ; Paracoccus denitrificans - genetics ; Protein Structure, Quaternary ; Protein Subunits ; Proteins ; Quinones ; Sequence Homology, Amino Acid ; Studies
É parte de: Proceedings of the National Academy of Sciences - PNAS, 2001-12, Vol.98 (25), p.14268-14273
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
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Present address: Department of Applied Chemistry, Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.
Edited by Perry A. Frey, University of Wisconsin, Madison, WI, and approved October 1, 2001
K. Tanizawa and F. S. Matthews are both senior authors of this paper.
To whom reprint requests should be addressed. E-mail: mathews@biochem.wustl.edu.
Descrição: The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from Paracoccus denitrificans has been determined at 2.05-A resolution. Within an 82-residue subunit is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified tryptophan side chain covalently linked to a nearby cysteine side chain. The subunit is surrounded on three sides by a 489-residue, four-domain subunit that includes a diheme cytochrome c. Both subunits sit on the surface of a third subunit, a 337-residue seven-bladed β-propeller that forms part of the enzyme active site. The small catalytic subunit is internally crosslinked by three highly unusual covalent cysteine to aspartic or glutamic acid thioether linkages in addition to the cofactor crossbridge. The catalytic function of the enzyme as well as the biosynthesis of the unusual catalytic subunit is discussed.
Editor: United States: National Academy of Sciences
Idioma: Inglês

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Structure of a Quinohemoprotein Amine Dehydrogenase with an Uncommon Redox Cofactor and Highly Unusual Crosslinking

Datta, Saumen ; Mori, Youichi ; Takagi, Kazuyoshi ; Kawaguchi, Katsunori ; Chen, Zhi-Wei ; Okajima, Toshihide ; Kuroda, Shun'ichi ; Ikeda, Tokuji ; Kano, Kenji ; Tanizawa, Katsuyuki ; Mathews, F. Scott

United States: National Academy of Sciences

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