Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy

phenol,NADH:oxygen oxidoreductase (2-hydroxylating)

phenol + NADH + H+ + O2 = catechol + NAD+ + H2O [RN:R10043]

R10043;
(other) R10042
Reaction

phenol [CPD:C00146];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]

The enzyme, characterized from the bacteria Pseudomonas sp. CF600 and Acinetobacter radioresistens, consists of a multisubunit oxygenease component that contains the active site and a dinuclear iron center, a reductase component that contains FAD and one iron-sulfur cluster, and a regulatory component. The reductase component is responsible for transferring electrons from NADH to the dinuclear iron center.

EC 1.14.13.244 created 2019

1  [PMID:2254258]

Nordlund I, Powlowski J, Shingler V

Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600.

J Bacteriol 172:6826-33 (1990)
DOI:10.1128/jb.172.12.6826-6833.1990

2  [PMID:2254259]

Powlowski J, Shingler V

In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600.

J Bacteriol 172:6834-40 (1990)
DOI:10.1128/jb.172.12.6834-6840.1990

3  [PMID:8995386]

Powlowski J, Sealy J, Shingler V, Cadieux E

On the role of DmpK, an auxiliary protein associated with multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600.

J Biol Chem 272:945-51 (1997)
DOI:10.1074/jbc.272.2.945

4  [PMID:9012665]

Qian H, Edlund U, Powlowski J, Shingler V, Sethson I

Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.

Biochemistry 36:495-504 (1997)
DOI:10.1021/bi9619233

5  [PMID:12186554]

Cadieux E, Vrajmasu V, Achim C, Powlowski J, Munck E

Biochemical, Mossbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600.

Biochemistry 41:10680-91 (2002)
DOI:10.1021/bi025901u