HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 24, 21381-21386, June 15, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/24/21381    most recent M101679200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kniemeyer, O. Articles by Heider, J. Search for Related Content PubMed PubMed Citation Articles by Kniemeyer, O. Articles by Heider, J. Social Bookmarking                      What's this?

Ethylbenzene Dehydrogenase, a Novel Hydrocarbon-oxidizing Molybdenum/Iron-Sulfur/Heme Enzyme^*

Olaf Kniemeyer and Johann Heider^§¶

From the  Max-Planck-Institut für marine Mikrobiologie, Celsiusstrasse 1, 28359 Bremen, and ^§ Mikrobiologie, Institut für Biologie II, Universität Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany

The initial enzyme of ethylbenzene metabolism in denitrifying Azoarcus strain EbN1, ethylbenzene dehydrogenase, was purified and characterized. The soluble periplasmic enzyme is the first known enzyme oxidizing a nonactivated hydrocarbon without molecular oxygen as cosubstrate. It is a novel molybdenum/iron-sulfur/heme protein of 155 kDa, which consists of three subunits (96, 43, and 23 kDa) in an structure. The N-terminal amino acid sequence of the  subunit is similar to that of other molybdenum proteins such as selenate reductase from the related species Thauera selenatis. Ethylbenzene dehydrogenase is unique in that it oxidizes the hydrocarbon ethylbenzene, a compound without functional groups, to (S)-1-phenylethanol. Formation of the product was evident by coupling to an enantiomer-specific (S)-1-phenylethanol dehydrogenase from the same organism. The apparent K_m of the enzyme for ethylbenzene is very low at <2 µM. Oxygen does not affect ethylbenzene dehydrogenase activity in extracts but inactivates the purified enzyme, if the heme b cofactor is in the reduced state. A variant of ethylbenzene dehydrogenase exhibiting significant activity also with the homolog n-propylbenzene was detected in a related Azoarcus strain (PbN1).

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				Y.-R. Chiang, W. Ismail, D. Heintz, C. Schaeffer, A. Van Dorsselaer, and G. Fuchs Study of Anoxic and Oxic Cholesterol Metabolism by Sterolibacterium denitrificans J. Bacteriol., February 1, 2008; 190(3): 905 - 914. [Abstract] [Full Text] [PDF]

				Y.-R. Chiang, W. Ismail, M. Muller, and G. Fuchs Initial Steps in the Anoxic Metabolism of Cholesterol by the Denitrifying Sterolibacterium denitrificans J. Biol. Chem., May 4, 2007; 282(18): 13240 - 13249. [Abstract] [Full Text] [PDF]

				S. Kuhner, L. Wohlbrand, I. Fritz, W. Wruck, C. Hultschig, P. Hufnagel, M. Kube, R. Reinhardt, and R. Rabus Substrate-Dependent Regulation of Anaerobic Degradation Pathways for Toluene and Ethylbenzene in a Denitrifying Bacterium, Strain EbN1 J. Bacteriol., February 15, 2005; 187(4): 1493 - 1503. [Abstract] [Full Text] [PDF]

				J. D. Van Hamme, A. Singh, and O. P. Ward Recent Advances in Petroleum Microbiology Microbiol. Mol. Biol. Rev., December 1, 2003; 67(4): 503 - 549. [Abstract] [Full Text] [PDF]

				H. D. Thorell, K. Stenklo, J. Karlsson, and T. Nilsson A Gene Cluster for Chlorate Metabolism in Ideonella dechloratans Appl. Envir. Microbiol., September 1, 2003; 69(9): 5585 - 5592. [Abstract] [Full Text] [PDF]

				O. Kniemeyer, T. Fischer, H. Wilkes, F. O. Glockner, and F. Widdel Anaerobic Degradation of Ethylbenzene by a New Type of Marine Sulfate-Reducing Bacterium Appl. Envir. Microbiol., February 1, 2003; 69(2): 760 - 768. [Abstract] [Full Text] [PDF]