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Originally published In Press as doi:10.1074/jbc.M109403200 on November 19, 2001

J. Biol. Chem., Vol. 277, Issue 5, 3727-3732, February 1, 2002
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Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni
STRUCTURAL BASIS FOR SUBSTRATE OXIDATION AND ELECTRON TRANSFER*

Arthur OubrieDagger §, Henriëtte J. RozeboomDagger , Kor H. Kalk, Eric G. Huizinga, and Bauke W. Dijkstra||

From the Laboratory of Biophysical Chemistry and BIOSON Research Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

Quinoprotein alcohol dehydrogenases are redox enzymes that participate in distinctive catabolic pathways that enable bacteria to grow on various alcohols as the sole source of carbon and energy. The x-ray structure of the quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni has been determined at 1.44 Å resolution. It comprises two domains. The N-terminal domain has a beta -propeller fold and binds one pyrroloquinoline quinone cofactor and one calcium ion in the active site. A tetrahydrofuran-2-carboxylic acid molecule is present in the substrate-binding cleft. The position of this oxidation product provides valuable information on the amino acid residues involved in the reaction mechanism and their function. The C-terminal domain is an alpha -helical type I cytochrome c with His608 and Met647 as heme-iron ligands. This is the first reported structure of an electron transfer system between a quinoprotein alcohol dehydrogenase and cytochrome c. The shortest distance between pyrroloquinoline quinone and heme c is 12.9 Å, one of the longest physiological edge-to-edge distances yet determined between two redox centers. A highly unusual disulfide bond between two adjacent cysteines bridges the redox centers. It appears essential for electron transfer. A water channel delineates a possible pathway for proton transfer from the active site to the solvent.

* This work was supported by the Netherlands Foundation for Chemical Research (CW) with financial aid from the Netherlands Organization for Scientific Research (NWO).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1KB0) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Dagger These authors contributed equally to this work.

§ Recipient of EMBO Long Term Fellowship ALTF57-2000. Present address: European Molecular Biology Laboratory, Structural and Computational Biology Program, Meyerhofstrasse 1, D-69117, Heidelberg, Germany.

Present address: Dept. of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.

|| To whom correspondence should be addressed. Tel.: 31-50-3634381; Fax: 31-50-3634800; E-mail: bauke@chem.rug.nl.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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