PMID- 26960184
OWN - NLM
STAT- MEDLINE
DCOM- 20161219
LR  - 20211203
IS  - 1660-2412 (Electronic)
IS  - 1464-1801 (Linking)
VI  - 26
IP  - 1-3
DP  - 2016
TI  - Ethylbenzene Dehydrogenase and Related Molybdenum Enzymes Involved in 
      Oxygen-Independent Alkyl Chain Hydroxylation.
PG  - 45-62
LID - 10.1159/000441357 [doi]
AB  - Ethylbenzene dehydrogenase initiates the anaerobic bacterial degradation of 
      ethylbenzene and propylbenzene. Although the enzyme is currently only known from 
      a few closely related denitrifying bacterial strains affiliated to the 
      Rhodocyclaceae, it clearly marks a universally occurring mechanism used for 
      attacking recalcitrant substrates in the absence of oxygen. Ethylbenzene 
      dehydrogenase belongs to subfamily 2 of the DMSO reductase-type molybdenum 
      enzymes together with paralogous enzymes involved in the oxygen-independent 
      hydroxylation of p-cymene, the isoprenoid side chains of sterols and even 
      possibly n-alkanes; the subfamily also extends to dimethylsulfide dehydrogenases, 
      selenite, chlorate and perchlorate reductases and, most significantly, 
      dissimilatory nitrate reductases. The biochemical, spectroscopic and structural 
      properties of the oxygen-independent hydroxylases among these enzymes are 
      summarized and compared. All of them consist of three subunits, contain a 
      molybdenum-bis-molybdopterin guanine dinucleotide cofactor, five Fe-S clusters 
      and a heme b cofactor of unusual ligation, and are localized in the periplasmic 
      space as soluble enzymes. In the case of ethylbenzene dehydrogenase, it has been 
      determined that the heme b cofactor has a rather high redox potential, which may 
      also be inferred for the paralogous hydroxylases. The known structure of 
      ethylbenzene dehydrogenase allowed the calculation of detailed models of the 
      reaction mechanism based on the density function theory as well as QM-MM (quantum 
      mechanics - molecular mechanics) methods, which yield predictions of mechanistic 
      properties such as kinetic isotope effects that appeared consistent with 
      experimental data.
CI  - (c) 2016 S. Karger AG, Basel.
FAU - Heider, Johann
AU  - Heider J
AD  - Laboratory of Microbial Biochemistry, LOEWE Center for Synthetic Microbiology, 
      Philipps University of Marburg, Marburg, Germany.
FAU - Szaleniec, Maciej
AU  - Szaleniec M
FAU - Sunwoldt, Katharina
AU  - Sunwoldt K
FAU - Boll, Matthias
AU  - Boll M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20160310
PL  - Switzerland
TA  - J Mol Microbiol Biotechnol
JT  - Journal of molecular microbiology and biotechnology
JID - 100892561
RN  - 0 (Alkanes)
RN  - 0 (Coenzymes)
RN  - 0 (Metalloproteins)
RN  - 0 (Molybdenum Cofactors)
RN  - 0 (Pteridines)
RN  - 97C5T2UQ7J (Cholesterol)
RN  - ATN6EG42UQ (molybdenum cofactor)
RN  - EC 1.- (Mixed Function Oxygenases)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.3.- (ethylbenzene dehydrogenase)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Alkanes/metabolism
MH  - Anaerobiosis
MH  - Bacteria, Anaerobic/enzymology
MH  - Biodegradation, Environmental
MH  - Cholesterol/chemistry/metabolism
MH  - Coenzymes/chemistry/*metabolism
MH  - Hydroxylation
MH  - Metalloproteins/chemistry/*metabolism
MH  - Mixed Function Oxygenases/chemistry/metabolism
MH  - Models, Molecular
MH  - Molybdenum Cofactors
MH  - Oxidoreductases/*chemistry/genetics/*metabolism
MH  - Oxygen/*metabolism
MH  - Pteridines/chemistry/*metabolism
MH  - Rhodocyclaceae/enzymology/metabolism
EDAT- 2016/03/10 06:00
MHDA- 2016/12/20 06:00
CRDT- 2016/03/10 06:00
PHST- 2016/03/10 06:00 [entrez]
PHST- 2016/03/10 06:00 [pubmed]
PHST- 2016/12/20 06:00 [medline]
AID - 000441357 [pii]
AID - 10.1159/000441357 [doi]
PST - ppublish
SO  - J Mol Microbiol Biotechnol. 2016;26(1-3):45-62. doi: 10.1159/000441357. Epub 2016 
      Mar 10.