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Literature summary for 1.14.13.172 extracted from

  • Rogers, M.S.; Lipscomb, J.D.
    Salicylate 5-hydroxylase intermediates in aromatic hydroxylation by a Rieske monooxygenase (2019), Biochemistry, 58, 5305-5319 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.172

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0029
-
 salicylate 23°C, pH not specified in the publication Ralstonia sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the reactive species that initiates catalysis appears to be an Fe(III)-superoxo species (or its electronic equivalent) which is made more reactive by the subsequent rapid transfer of an electron from the Rieske cluster. This transfer promotes O-O bond cleavage and drives the product forming reaction to completion Ralstonia sp.

Organism

Organism UniProt Comment Textmining
Ralstonia sp. O52378 and O52381 and O52379 and O52380 O52378 i.e. reductase component NagAa, O52381 i.e. ferredoxin component NagAb cf. EC 1.18.1.7, O52379 i.e. large oxygenase component NagH, O52380 i.e. small oxygenase component NagH
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
salicylate + NADH + H+ + O2
-
 Ralstonia sp. 2,5-dihydroxybenzoate + NAD+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
S5HR
-
 Ralstonia sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.64
-
 salicylate 4°C, pH not specified in the publication Ralstonia sp.
1.86
-
 salicylate 23°C, pH not specified in the publication Ralstonia sp.

General Information

General Information Comment Organism
metabolism binding of salicylate and O2 is fast. Transfer of the Rieske electron required to form the gentisate product occurs through bonds over about 12 A and must also be very fast. The observed rate constant for this reaction is much slower than expected and sensitive to substrate type. A transient intermediate (lambdamax of 700 nm) with an EPR resonance at g 4.3 is observed after product is formed in the active site. Gentisate binds to the mononuclear iron via its C5-OH in the intermediate. Rereduction of the metal centers accelerates product release about 300fold Ralstonia sp.