Purification and some properties of a soluble benzene-oxidizing system from a strain of <i>Pseudomonas</i>

Axcell, B. C.; Geary, P. J.

doi:10.1042/bj1460173

Cited by 155 publications

(76 citation statements)

References 13 publications

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“…The discovery of two other bacterial oxygenases [17,18] with ESR properties analogous to those of thc g = 1.89 clusters and the finding that Fe(1I) ions are necessary for full activity support our suggestion.…”

Section: Iron-sulfur Clusters Of Putidamonooxinsupporting

confidence: 72%

An Electron-Spin-Resonance Study on the Reodex-Active Centers of the 4-Methoxybenzoate Monooxygenase from Pseudomonas putida

1981

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4-Methoxybenzoate monooxygenase isolated from a species of Pseudomonas putida can be separated in two components, NADH-putidamonooxin oxidoreductase and putidamonooxin, the latter contains the dioxygenactivating site. Binding of tight coupling substrates leads to monooxygenase activity of this enzyme system with substrate hydroxylation, whereas binding of uncoupling substrates leads to oxidase activity with production The NADH-putidamonooxin oxidoreductase when reduced with NADH exhibits an electron spin resonance (ESR) spectrum with rhombic symmetry and an isotropic resonance at g = 2.0033. The average g value of 1.96 and the temperature behaviour of the rhombic spectrum are indicative for (2Fe-2s) clusters. In the range of pH 6.8-8.2 the isotropic ESR signal attributed to FMN shows the characteristic linewidth of the blue semiquinone form.The reduced putidamonooxin shows an ESR spectrum with rhombic symmetry and an average g value of 1.89 caused by a pronounced g anisotropy. An identical g anisotropy is observed for the Rieske-cluster.The "Fe-enriched (2Fe-2s) clusters show hyperfine interaction between the electron spin and the nuclear spin of the iron atoms in two principal directions of the A-tensor, the resonance in the third direction is not resolved. For one direction equivalent hyperfine constants with a = 1.23 mT are observed, whereas for the other direction the hyperfine constants are inequivalent with a = 2.0 mT and a < 0.05 mT respectively indicating different spin densities at the iron atoms in the cluster. Hyperfine constants and g tensor of the reduced cluster are not influenced by binding of substrate to putidamonooxin.The ESR feature in the range of g = 9.6 -4.3 is characteristic for a mononuclear non-heme iron center in oxidized putidamonooxin. The temperature behaviour of the resonance at g5 = 4.293 in the range of 3.6-80 K indicates a zero-field splitting with D = 0.9 0.1 cm-'. Therefore, we assume that this iron center is probably coordinated by oxygen and nitrogen atoms. On the basis of g values this mononuclear non-heme iron center has at least two different microenvironments generating rhombic ( E / D = 0.33) and tetragonal symmetry (E/D = 0.05 -0.15). Whereas the iron with tetragonal symmetry is sensitive to substrate-binding, the iron with rhombic symmetry seems to be independent of substrate-binding. Nevertheless, both symmetry species are involved in the activation of dioxygen as the iron-sulfur clusters can only be aerobically oxidized if mononuclear iron centers are present in a 1 : 1 ratio. Substitution of the mononuclear non-heme iron center by 57Fe leads to a line-broadening of the resonance at g5 = 4.293 indicating a splitting constant of 0.8 5 0.2 mT.It is excluded, by comparing aerobically and anaerobically oxidized putidamonooxin, that the iron center with tetragonal symmetry belongs to a ternary dioxygen ' enzyme . substrate complex. of H202.

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Section: Iron-sulfur Clusters Of Putidamonooxinsupporting

confidence: 72%

An Electron-Spin-Resonance Study on the Reodex-Active Centers of the 4-Methoxybenzoate Monooxygenase from Pseudomonas putida

1981

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“…These results indicate that anilines are degraded via catechols in strain YAA, and this pathway is consistent with previous studies (Aoki et al, 1983;Lyons et al, 1984). We were unable to detect the presence of cis-diol compounds which are found as precursors of catechol in aromatic compound oxidation (Gibson et al, 1970;Axcell & Geary, 1975;Shirai, 1986;Eaton & Timmis, 1986) by GC-MS analyses.…”

Section: Restriction Endonuclease Analysis Of Pas185mentioning

confidence: 92%

Plasmid-Encoded Genes Specifying Aniline Oxidation from Acinetobacter sp. Strain YAA

Fujii

Takeo

Maeda³

1997

Microbiology

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Acinetobacter sp. strain YAA is able to use aniline and o-toluidine as the sole carbon and energy source. This strain has several different plasmids and acridine orange curing suggested that aniline utilization in strain YAA was Sall fragment from the insert in E. coli resulted in the accumulation of catechol. Southern hybridization studies indicated that the aniline oxygenase gene (atdA) was present on one of the plasmids, pYA1. These results suggest that in strain YAA aniline is degraded via catechol through a pathway involving meta-cleavage of the benzene-ring by plasmid-encoded genes including atdA.

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“…capsulatus (Bath) [2,91, the benzoate dioxygenase of Pseudomonas arvilla [ 191, the 4-methoxybenzoate 0-demethylase of Pseudomonas putida 1201 and the microsomal P-450 monooxygenase 1221; or the two redox centres may be separate on two components, as for the benzene dioxygenase of P. putida [22], the camphor hydroxylase of P . putida [23,24], the alkane hydroxylase of Pseudomonas oleovorans [25], or the mitochondria1 P-450 monooxygenase [25].…”

Section: Discussionmentioning

confidence: 99%

Electron transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath)

Lund

Woodland

Dalton

1985

European Journal of Biochemistry

127

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1. Aerobic stopped-flow experiments have confirmed that component C is the methane monooxygenase component responsible for interaction with NADH. Reduction of component C by NADH is not the rate-limiting step for component C in the methane monooxygenase reaction.2. Removal and reconstitution of the redox centres of component C suggests a correlation between the presence of the FAD and Fe2S2 redox centres and NADH: acceptor reductase activity and methane monooxygenase activity respectively, consistent with the order of electron flow: NADH + FAD + Fe2S2 4 component A. This order suggests that component C functions as a 2e-'/le-' transformase, splitting electron pairs from NADH for transfer to component A via the one-electron-carrying Fe2S2 centre.3. Electron transfer has been demonstrated between the reductase component, component C and the oxygenase component, component A, of the methane monooxygenase complex from Methylococcus capsulatus (Bath) by three separate methods. This intermolecular electron transfer step is not rate-determining for the methane monooxygenase reaction.4. Intermolecular electron transfer was independent of component B, the third component of the methane monooxygenase. Component B is required to switch the oxidase activity of component A to methane monooxygenase activity, suggesting that the role of component B is to couple substrate oxidation to electron transfer, via the methane monooxygenase components.

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Purification and some properties of a soluble benzene-oxidizing system from a strain of Pseudomonas

Cited by 155 publications

References 13 publications

An Electron-Spin-Resonance Study on the Reodex-Active Centers of the 4-Methoxybenzoate Monooxygenase from Pseudomonas putida

An Electron-Spin-Resonance Study on the Reodex-Active Centers of the 4-Methoxybenzoate Monooxygenase from Pseudomonas putida

Plasmid-Encoded Genes Specifying Aniline Oxidation from Acinetobacter sp. Strain YAA

Electron transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath)

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