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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1993-5-21
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pubmed:abstractText |
The reductive removal of aromatic hydroxyl functions plays an important role in the anaerobic metabolism of many phenolic compounds. We describe a new enzyme from a denitrifying Pseudomonas sp., 4-hydroxybenzoyl-CoA reductase (dehydroxylating), which reductively dehydroxylates 4-hydroxybenzoyl-CoA to benzoyl-CoA. The enzyme plays a role in the anaerobic degradation of phenol, 4-hydroxybenzoate, p-cresol, 4-hydroxyphenylacetate, and other aromatic compounds of which 4-hydroxybenzoyl-CoA is an intermediate. The enzyme is therefore induced only under anoxic conditions with these aromatic substrates, but not with benzoate or under aerobic conditions. A similar enzyme which reductively dehydroxylates 3-hydroxybenzoyl-CoA is induced during anaerobic growth with 3-hydroxybenzoate. The soluble enzyme 4-hydroxybenzoyl-CoA reductase was purified. It has a molecular mass of 260 kDa and consists of three subunits of 75, 35, and 17 kDa. The subunit composition is likely to be a2b2c2. The enzyme contains 12 mol iron/mol and 12 mol acid-labile sulfur/mol and exhibits a typical ultraviolet/visible spectrum of an iron-sulfur protein. The reaction requires a reduced electron donor such as reduced viologen dyes; no other co-catalysts are required, the product is benzoyl-CoA and oxidized dye. The reductase is rapidly inactivated by oxygen. The inactivation by low concentrations of cyanide or azide in a pseudo-first-order time course suggests that it may contain a transition metal in an oxidation state which reacts with these ligands. 4-Hydroxybenzoyl-CoA reductase represents a type of enzyme which is common in anaerobic aromatic metabolism of phenolic compounds. A similar enzyme is demonstrated in Rhodopseudomonas palustris anaerobically grown with 4-hydroxybenzoate. The biological significance of reductive dehydroxylation of aromatics and a possible reaction mechanism similar to the Birch reduction are discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on CH-CH...,
http://linkedlifedata.com/resource/pubmed/chemical/Phenols,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur,
http://linkedlifedata.com/resource/pubmed/chemical/benzoyl-coenzyme A-4-oxidoreductase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
213
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
563-71
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:8477729-Amino Acid Sequence,
pubmed-meshheading:8477729-Catalysis,
pubmed-meshheading:8477729-Chromatography,
pubmed-meshheading:8477729-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8477729-Enzyme Stability,
pubmed-meshheading:8477729-Hydroxylation,
pubmed-meshheading:8477729-Iron,
pubmed-meshheading:8477729-Molecular Sequence Data,
pubmed-meshheading:8477729-Oxidoreductases,
pubmed-meshheading:8477729-Oxidoreductases Acting on CH-CH Group Donors,
pubmed-meshheading:8477729-Phenols,
pubmed-meshheading:8477729-Pseudomonas,
pubmed-meshheading:8477729-Spectrophotometry, Ultraviolet,
pubmed-meshheading:8477729-Substrate Specificity,
pubmed-meshheading:8477729-Sulfur
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pubmed:year |
1993
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pubmed:articleTitle |
Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species.
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pubmed:affiliation |
Angewandte Mikrobiologie, Universität Ulm, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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