Chloroperoxidase

Thomas, John A.; Morris, David R.; Hager, Lowell P.

doi:10.1016/s0021-9258(18)63033-9

Cited by 128 publications

(25 citation statements)

References 20 publications

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“…The latter complex shows a 2-3-nm red shift in the Soret band. These results compare closely with the pH properties of the Soret band absorbance of other peroxidases such as myleoperoxidase and chloroperoxidase (Stelmaszynska & Zgliczynski, 1974;Thomas et al, 1970b). Other peroxidases such as lactoperoxidase and hog intestinal peroxidase show no difference in the Soret band spectra of the acid and acid-halide complexes (Kimura & Yamazaki, 1978).…”

Section: Resultssupporting

confidence: 75%

Characterization of the catalytic properties of bromoperoxidase

Manthey¹,

Hager²

1989

Biochemistry

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Bromoperoxidase from the marine green alga Penicillus capitatus is a soluble heme protein capable of catalyzing the peroxidation of a wide variety of organic and inorganic substrates. Bromoperoxidase at neutral p H has high specific activity for bromide and iodide oxidations. The V,,, values for bromide and iodide oxidations are 5900 and 35000 mol m i d (mol of BP0)-', respectively. At acidic pH, bromoperoxidase catalyzes the oxidation of chloride ion. Radiolabeling experiments demonstrate the ability of the enzyme to catalyze chloride ion oxidation and insertion of chloride into the halide acceptor molecule monochlorodimedone. The rates of several reactions catalyzed by bromoperoxidase are strongly enhanced by bromide and chloride ions. The rate of molecular bromine formation is nearly twice the rate of bromination of monochlorodimedone. Thus, bromination is proposed to occur via molecular bromine rather than via an enzyme-bound intermediate. The pH-rate profiles for bromide and chloride ion oxidations provide new insights for possible control mechanisms for halide ion peroxidations.Bromoperoxidase purified from the marine alga Penicillus capitatus is a heme-containing peroxidase that shares many spectral and catalytic properties with other plant and mammalian peroxidases. The spectra of the oxidized and reduced derivatives of bromoperoxidase closely resemble the spectra of those peroxidases which have a proximal histidine ligand to the heme iron. In the presence of peroxides, bromoperoxidase forms the two classical peroxidase intermediates, compounds I and 11, which contain 2 and 1 oxidizing equiv above native enzyme. These intermediates are capable of proceding through the one-electron donor peroxidative cycle shown in eq 1-4. native enzyme + ROOH -compound I + ROH (1) compound I + AH -compound I1

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Section: Resultssupporting

confidence: 75%

Characterization of the catalytic properties of bromoperoxidase

Manthey¹,

Hager²

1989

Biochemistry

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“…As described above, through the measured addition of single-electron reducing equivalents of veratryl alcohol and other substrates, it is possible to reduce lignin peroxidase compound I to compound II and then to the native enzyme, thus completing a peroxidase catalytic cycle (Figure 6). This indicates that the enzyme dehydrogenates veratryl alcohol via two single-electron oxidation steps rather than via a single two-electron step mechanism as observed with CAT and CPO (Schonbaum & Chance, 1976;Thomas et al, 1970). An early assay for lignin peroxidase was the oxidation of KTBA to produce ethylene (Glenn et al, 1983;Gold et al, 1983).…”

Section: Discussionmentioning

confidence: 72%

“…In the presence of H202, lignin peroxidase oxidizes veratryl alcohol to veratryl aldehyde (Kuwahara et al, 1984;Tien & Kirk, 1984). In this respect, it shares the ability of CAT and CPO (Schonbaum & Chance, 1976;Thomas et al, 1970;Giegert et al, 1983) to dehydrogenate some alcohols. Alcohol dehydrogenation is not observed with HRP, lactoperoxidase, or myeloperoxidase (Geigert et al, 1983).…”

Section: Discussionmentioning

confidence: 99%

Spectral characterization of the oxidized states of lignin peroxidase, an extracellular heme enzyme from the white rot basidiomycete Phanerochaete chrysosporium

Renganathan¹,

Gold²

1986

Biochemistry

187

114

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“…Additional UPOs have been isolated from cultures of the basidiomycetes Coprinellus radians ( Cra UPO), Marasmius rotula ( Mro UPO), and Marasmius wettsteinii ( Mwe UPO) and the ascomycete Chaetomium globosum ( Cgl UPO) . The classical chloroperoxidase from Leptoxyphium fumago also belongs to the same protein family, although it exhibits low oxygenation and high halogenation activities compared with UPOs …”

Section: Introductionmentioning

confidence: 99%

Modulating Fatty Acid Epoxidation vs Hydroxylation in a Fungal Peroxygenase

et al. 2019

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Unspecific peroxygenases (UPOs) are fungal secreted counterparts of the cytochrome P450 monooxygenases present in most living cells. Both enzyme types share the ability to perform selective oxygenation reactions. Moreover, the Marasmius rotula UPO (MroUPO) catalyzes reactions of interest compared with the previously described UPOs, including formation of reactive epoxy fatty acids. To investigate substrate epoxidation, the most frequent positions of oleic acid at the MroUPO heme channel were predicted using binding and molecular dynamics simulations. Then, mutations in neighbor residues were designed aiming at modulating the enzyme epoxidation vs hydroxylation ratio. Both the native (wild-type recombinant) MroUPO and the mutated variants were expressed in Escherichia coli as active enzymes, and their action on oleic and other fatty acids was investigated by gas chromatography–mass spectrometry in combination with kinetic analyses. Interestingly, a small modification of the channel shape in the I153T variant increased the ratio between epoxidized oleic acid and its additionally hydroxylated derivatives. A fully opposite effect was attained with the double I153F/S156F variant that completely abolished the ability of the MroUPO to epoxidize oleic acid (while no activity was detected for the I153V variant). The rationale for these results was revealed by the substrate positioning in the above computational simulations, which predict a shorter distance between the oleic acid double bond and the oxygen atom of the peroxide-activated heme (compound I) in the I153T variant than in the native enzyme, promoting epoxidation. In contrast, the I153F/S156F double mutation fully prevents the approach of oleic acid in the bent conformation required for double-bond epoxidation, although its (sub)terminal hydroxylation was predicted and experimentally confirmed. The I153T mutation also increased the UPO selectivity on polyunsaturated fatty acid epoxidation, strongly reducing the ratio between simple epoxides and their hydroxylated derivatives, with respect to the native UPO.

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Chloroperoxidase

Cited by 128 publications

References 20 publications

Characterization of the catalytic properties of bromoperoxidase

Characterization of the catalytic properties of bromoperoxidase

Spectral characterization of the oxidized states of lignin peroxidase, an extracellular heme enzyme from the white rot basidiomycete Phanerochaete chrysosporium

Modulating Fatty Acid Epoxidation vs Hydroxylation in a Fungal Peroxygenase

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