Oxygen-Independent Decarbonylation of Aldehydes by Cyanobacterial Aldehyde Decarbonylase: A New Reaction of Diiron Enzymes
- Authors
- Das, Debasis; Eser, Bekir E.; Han, Jaehong; Sciore, Aaron; Marsh, E. Neil G.
- Issue Date
- 25-Jul-2011
- Publisher
- WILEY-V C H VERLAG GMBH
- Keywords
- biofuels; free radicals; hydrolysis reactions; metalloproteins; radical traps
- Citation
- ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, v.50, no.31, pp 7148 - 7152
- Pages
- 5
- Journal Title
- ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Volume
- 50
- Number
- 31
- Start Page
- 7148
- End Page
- 7152
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/21969
- DOI
- 10.1002/anie.201101552
- ISSN
- 1433-7851
1521-3773
- Abstract
- Just add water: Structurally, cyanobacterial aldehyde decarbonylases are members of the non-heme diiron oxygenase family of enzymes. However, the enzyme catalyzes the hydrolysis of aliphatic aldehydes to alkanes and formate (see scheme), in an oxygen-independent reaction. This unusual and chemically difficult reaction most likely involves free radical intermediates. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Collections - College of Biotechnology & Natural Resource > ETC > 1. Journal Articles
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