Publikation: Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase
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2007
Autor:innen
Seiffert, Grażyna Bernadeta
Ullmann, G. Matthias
Messerschmidt, Albrecht
Schink, Bernhard
Kroneck, Peter M. H.
Einsle, Oliver
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Proceedings of the National Academy of Sciences of the United States of America. 2007, 104(9), pp. 3073-3077
Zusammenfassung
The tungsten iron sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 Å now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pKa of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.
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570 Biowissenschaften, Biologie
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acetylene reduction, metalloproteins, tungsten enzymes
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SEIFFERT, Grażyna Bernadeta, G. Matthias ULLMANN, Albrecht MESSERSCHMIDT, Bernhard SCHINK, Peter M. H. KRONECK, Oliver EINSLE, 2007. Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase. In: Proceedings of the National Academy of Sciences of the United States of America. 2007, 104(9), pp. 3073-3077BibTex
@article{Seiffert2007Struc-7218,
year={2007},
title={Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase},
number={9},
volume={104},
journal={Proceedings of the National Academy of Sciences of the United States of America},
pages={3073--3077},
author={Seiffert, Grażyna Bernadeta and Ullmann, G. Matthias and Messerschmidt, Albrecht and Schink, Bernhard and Kroneck, Peter M. H. and Einsle, Oliver}
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<dcterms:abstract xml:lang="eng">The tungsten iron sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 Å now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pKa of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.</dcterms:abstract>
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