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9-fluorenone + NAD(P)H + H+ + O2
1,1a-dihydroxy-1-hydrofluoren-9-one + NAD(P)+
-
-
angular dioxygenation, yield 8-12%
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
anthracene + NADH + H+ + O2
?
biphenyl + NAD(P)H + H+ + O2
2-hydroxybiphenyl + 3-hydroxybiphenyl + biphenyl dihydrodiol + NAD(P)+
-
-
in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc, ratio of products depends on reaction time. Synthesis of up to 46% biphenyl dihydrodiol
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + 2-hydroxybiphenyl + 3-hydroxybiphenyl + NAD(P)+
-
-
lateral dioxygenation to cis-2,3-dihydroxy-2,3-dihydrobiphenyl, yield 85-90%, and to dihydrodiol, yield 9-11%
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
biphenyl + NADH + H+ + O2
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
dibenzo-p-dioxin + NAD(P)H + H+ + O2
2,2',3-trihydroxybiphenyl ether + NAD(P)+
-
-
26% 2,2',3-trihydroxybiphenyl ether in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenyl ether + NAD(P)+
-
-
-
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
? + NAD(P)+
dibenzofuran + NAD(P)H
? + NAD(P)+
dibenzofuran + NAD(P)H + H+ + O2
2,2',3-trihydroxybiphenyl + NAD(P)+
dibenzofuran + NADH + H+ + O2
2,2',3-trihydroxybiphenyl + NAD+
-
-
-
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
dibenzothiophene + NADH + H+ + O2
?
dibenzothiophene + NADH + H+ + O2
dibenzothiophene 5-oxide + NAD+
-
-
-
-
?
dibenzothiophene + NADH + H+ + O2
dibenzothiophene sulfoxide + NAD+ + H2O
-
-
monooxygenation, yield 99-100%
-
?
dibenzo[1,4]dioxin + NADH + H+ + O2
?
-
-
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + NAD(P)+
-
poor substrate
-
-
?
fluoranthene + NADH + H+ + O2
?
fluorene + NAD(P)H + H+ + O2
9-fluorenol + ? + NAD(P)+
-
-
monooxygenation to 9-fluorenol, yield 3-5%, and lateral dioxygenation to dihydrodiol, yield 5-8%
-
?
fluorene + NAD(P)H + H+ + O2
9-fluorenone + 9-fluorenol + monohydroxyfluorene + fluorene dihydrodiol + NAD(P)+
-
-
in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc, ratio of products depends on reaction time
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
fluorene + NADH + H+ + O2
9-fluorenone + NAD+
-
-
-
-
?
fluorene + NADH + H+ + O2
?
-
-
-
?
N-ethylcarbazole + NAD(P)H + H+ + O2
? + NAD(P)+
-
-
-
?
N-methylcarbazole + NAD(P)H + H+ + O2
? + NAD(P)+
-
-
-
?
naphthalene + NAD(P)H + H+ + O2
1-naphthol + cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD(P)+
-
-
7.3% 1-naphthol and 93% cis-1,2-dihydroxy-1,2-dihydronaphthalene in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
naphthalene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + 1-naphthol + NAD(P)+
-
-
lateral dioxygenation, yield 65-70%
-
?
naphthalene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD(P)+
naphthalene + NADH + H+ + O2
?
phenanthrene + NAD(P)H + H+ + O2
? + NAD(P)+
phenanthrene + NAD(P)H + H+ + O2
phenanthrene dihydrodiol + monohydroxyphenanthrene + NAD(P)+
-
-
70% phenanthrene dihydrodiol and 9% monohydroxyphenanthrene in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
phenanthrene + NADH + H+ + O2
?
-
-
-
-
?
phenazine + NAD(P)H + H+ + O2
? + NAD(P)+
-
-
-
?
phenothiazine + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 7.6% substrate remaining
-
-
?
phenoxathiin + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenyl sulfide + NAD(P)+
phenoxazine + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 1.1% substrate remaining
-
-
?
pyrene + NADH + H+ + O2
?
-
-
-
-
?
xanthene + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenylmethane + NAD(P)+
additional information
?
-
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
-
?
9H-carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
-
?
9H-carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
18 h reaction time, 8.7% substrate remaining
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
-
-
-
-
?
anthracene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydroanthracene + NAD(P)+
18 h reaction time, 8.7% substrate remaining
-
-
?
anthracene + NADH + H+ + O2
?
-
-
-
?
anthracene + NADH + H+ + O2
?
-
-
-
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
-
-
cis dihydroxylation
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
18 h reaction time, 0% substrate remaining
-
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
-
-
cis dihydroxylation
-
?
biphenyl + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrobiphenyl + NAD(P)+
18 h reaction time, 0% substrate remaining
-
-
?
biphenyl + NADH + H+ + O2
?
-
-
-
?
biphenyl + NADH + H+ + O2
?
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
100% 2'-aminobiphenyl-2,3-diol in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
best substrate
angular dioxygenation, yield 70-80%
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
18 h reaction time, 1.3% substrate remaining
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
18 h reaction time, 1.3% substrate remaining
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
-
-
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
about 80% conversion in Escherichia coli harboring genes car-AaAcfdr
-
?
carbazole + NAD(P)H + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD(P)+
-
about 80% conversion in Escherichia coli harboring genes car-AaAcfdr
-
?
carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADH + H+ + O2
2'-aminobiphenyl-2,3-diol + NAD+
-
-
-
?
carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
carbazole + NADPH + H+ + O2
2'-aminobiphenyl-2,3-diol + NADP+
-
-
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 3.9% substrate remaining
-
-
?
dibenzo-p-dioxin + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 3.9% substrate remaining
-
-
?
dibenzofuran + NAD(P)H
? + NAD(P)+
18 h reaction time, 48.5% substrate remaining
-
-
?
dibenzofuran + NAD(P)H
? + NAD(P)+
18 h reaction time, 48.5% substrate remaining
-
-
?
dibenzofuran + NAD(P)H + H+ + O2
2,2',3-trihydroxybiphenyl + NAD(P)+
-
-
74% 2,2',3-trihydroxybiphenyl in Escherichia coli expressing terminal oxygenase gene CarAa and ferredoxin component gene CarAc
-
?
dibenzofuran + NAD(P)H + H+ + O2
2,2',3-trihydroxybiphenyl + NAD(P)+
-
-
angular dioxygenation, yield 60-65%
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
-
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
-
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
monooxygenation
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
-
-
?
dibenzothiophene + NAD(P)H + H+ + O2
dibenzothiophene-5-oxide + NAD(P)+
-
-
monooxygenation
-
?
dibenzothiophene + NADH + H+ + O2
?
-
-
-
?
dibenzothiophene + NADH + H+ + O2
?
-
-
-
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
-
-
-
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
-
-
-
?
fluoranthene + NAD(P)H + H+ + O2
cis-2,3-dihydroxy-2,3-dihydrofluoranthene + monohydroxyfluoranthene + NAD(P)+
-
-
-
-
?
fluoranthene + NADH + H+ + O2
?
-
-
-
-
?
fluoranthene + NADH + H+ + O2
?
-
-
-
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
-
-
-
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
-
-
monooxygenation
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
18 h reaction time, 80.8% substrate remaining
-
-
?
fluorene + NAD(P)H + H+ + O2
9-hydroxyfluorene + NAD(P)+
-
-
monooxygenation
-
?
naphthalene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD(P)+
-
-
cis dihydroxylation
-
?
naphthalene + NAD(P)H + H+ + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD(P)+
18 h reaction time, 23.6% substrate remaining
-
-
?
naphthalene + NADH + H+ + O2
?
-
-
-
?
naphthalene + NADH + H+ + O2
?
-
-
-
-
?
phenanthrene + NAD(P)H + H+ + O2
? + NAD(P)+
-
-
products are three dihydrodiols
-
?
phenanthrene + NAD(P)H + H+ + O2
? + NAD(P)+
18 h reaction time, 5.4% substrate remaining
-
-
?
phenoxathiin + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenyl sulfide + NAD(P)+
-
-
angular dioxygenation by CARDO occurs at the angular position adjacent to the oxygen atom to yield hetero ring-cleaved compounds
-
?
phenoxathiin + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenyl sulfide + NAD(P)+
18 h reaction time, 25% substrate remaining
-
-
?
xanthene + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenylmethane + NAD(P)+
-
-
angular dioxygenation
-
?
xanthene + NAD(P)H + H+ + O2
2,2',3-trihydroxydiphenylmethane + NAD(P)+
18 h reaction time, 52.8% substrate remaining
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
terminal oxygenase subunit CarAa is reduced by His-tagged ferredoxin CarAc, His-tagged ferredoxin reductase CarAd, and NADH. The three purified proteins can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. Terminal oxygenase subunit CarAa is reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
in the presence of NADH, His-tagged ferrdoxin subunit CarAc is reduced by His-tagged ferredoxin reductase CarAd. The three purified proteins CarAa, CarAc and CarAd can reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc is indispensable for electron transport, while His-tagged CarAd can be replaced by some unrelated reductases
-
-
?
additional information
?
-
-
the enzyme does not degrade alkanes like pentadecane, hexadecane, heptadecane, octadecane, nonadecane and docosane
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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crystal structures of the reduced carbazole-bound, dioxygen-bound, and both carbazole- and dioxygen-bound subunits CARDO-O:CARDO-F binary complex structures at 1.95, 1.85, and 2.00 A resolution, using the catalytic terminal oxygenase subunit from Janthinobacterium sp. J3 and ferredoxin from Pseudomonas resinovorans CA10. Catalytic mechanism is as follows: When the Rieske cluster is reduced, substrate binding induces several conformational changes that create room for oxygen binding. Dioxygen bound in a side-on fashion onto nonheme iron is activated by reduction to the peroxo state [Fe(III)-(hydro)peroxo]. This state may react directly with the bound substrate, or OO bond cleavage may occur to generate Fe(V)-oxo-hydroxo species prior to the reaction. After producing a cis-dihydrodiol, the product is released by reducing the nonheme iron
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
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crystal structure of oxygenase component CARDO-O at a resolution of 1.95 A, and of selenomethione derivative to 2.3 A resolution. The alpha3 trimeric overall structure of the CARDO-O molecule roughly corresponds to the alpha3 partial structures of other terminal oxygenase components of Rieske non-heme iron oxygenase systems that have the alpha3beta3 configuration and reveals the presence of the specific loops that interact with a neighboring subunit. The shape of the substrate-binding pocket of CARDO-O is markedly different from those of other oxygenase components involved in naphthalene and biphenyl degradation pathways. Docking simulations suggest that carbazole binds to the substrate-binding pocket in a manner suitable for catalysis of angular dioxygenation
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crystal structures of the nonreduced, reduced, and substrate-bound binary complexes of terminal oxygenase CARDO-O from Janthinobacterium sp. J3 with its electron donor, ferredoxin CARDO-F from Pseudomonas resinovorans CA10 at 1.9, 1.8, and 2.0 A resolutions, respectively. The structures provide a structure-based interpretation of intercomponent electron transfer between two Rieske [2Fe-2S] clusters of ferredoxin and oxygenase in a Rieske nonheme iron oxygenase system. Three molecules of CARDO-F bind to the subunit boundary of one CARDO-O trimeric molecule, and specific binding created by electrostatic and hydrophobic interactions with conformational changes suitably aligns the two Rieske clusters for electron transfer. Additionally, conformational changes upon binding carbazole results in the closure of a lid over the substrate-binding pocket, thereby seemingly trapping carbazole at the substrate-binding site
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crystallization of ferredoxin reductase subunit CARDO-R using the hanging-drop vapour-diffusion method with the precipitant PEG 8000 results in two crystal types. The type I crystal diffract to a maximum resolution of 2.80 A and belong to space group P42212, with unit cell parameters a, b of 158.7, c of 81.4 A. The type II crystal diffracts to 2.60 A resolution and belongs to the same space group, with unit-cell parameters a, b of 161.8, c of 79.5 A
docking simulation of dibenzo-p-dioxin to wild-type CARDO oxygenase
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hanging drop vapor diffusion method, using 0.1M ammonium acetate, 12.5% (w/v) polyethylene glycol 3350 in 0.05 M MES at pH 5.5-5.7
hanging drop vapor diffusion method, using 14% (w/v) PEG 3350, 0.1 M sodium cacodylate pH 5.7
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comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
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crystallization of ferredoxin component, to 2.0 A resolution, space group P41212
terminal oxygenase component, to 2.3 A resolution, space group C2
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
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crystal structure of ferredoxin component CarAc at 1.9 A resolution by molecular replacement using the structure of BphF, the biphenyl 2,3-dioxygenase ferredoxin from Burkholderia cepacia strain LB400 as a search model. CarAc is composed of three beta-sheets, and the structure can be divided into a cluster-binding domain and a basal domain. The Rieske [2Fe-2S] cluster is located at the tip of the cluster-binding domain, where it is exposed to solvent. While the overall folding of CarAc and BphF is strongly conserved, the properties of their surfaces are very different from each other. The structure of the cluster-binding domain of CarAc is more compact and protruding than that of BphF
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crystal structures of the nonreduced, reduced, and substrate-bound binary complexes of terminal oxygenase CARDO-O from Janthinobacterium sp. J3 with its electron donor, ferredoxin CARDO-F from Pseudomonas resinovorans CA10 at 1.9, 1.8, and 2.0 A resolutions, respectively. The structures provide a structure-based interpretation of intercomponent electron transfer between two Rieske [2Fe-2S] clusters of ferredoxin and oxygenase in a Rieske nonheme iron oxygenase system. Three molecules of CARDO-F bind to the subunit boundary of one CARDO-O trimeric molecule, and specific binding created by electrostatic and hydrophobic interactions with conformational changes suitably aligns the two Rieske clusters for electron transfer. Additionally, conformational changes upon binding carbazole results in the closure of a lid over the substrate-binding pocket, thereby seemingly trapping carbazole at the substrate-binding site
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CARDO of Novosphingobium sp. KA1 consists of a terminal oxygenase, a putidaredoxin-type ferredoxin and a ferredoxin-NADH oxidoreductase. Crystallization of the ferredoxin reductase component to 1.58 A resolution, space group P32, with unit-cell parameters a = b = 92.2, c = 78.6 A
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CARDO of Novosphingobium sp. KA1 consists of a terminal oxygenase, Oxy, a putidaredoxin-type ferredoxin and a ferredoxin-NADH oxidoreductase. Crystallization of the oxygenase component to 2.1 A resolution, space group P21
comparison of crystal structures of the oxygenase and ferredoxin components to the CARDOs from Pseudomonas resinovorans CA10, Janthinobacterium sp. J3, Novosphingobium sp. KA1, and Nocardioides aromaticivorans IC177 which are grouped into classes III, III, IIA, and IIB, respectively. The comparison suggests residues in common between class IIB and class III CARDOs that are important for interactions between ferredoxin and oxygenase. In the class IIB CARDOs, these include His75 and Glu71 in ferredoxin and Lys20 and Glu357 in the oxygenase for electrostatic interactions, and Phe74 and Pro90 in ferredoxin and Trp21, Leu359, and Val367 in the oxygenase for hydrophobic interactions
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