Purification and characterization of a novel metal-containing nonheme bromoperoxidase from Pseudomonas putida

Itoh, Nobuhide; Morinaga, Naoki; Kouzai, Toyoko

doi:10.1016/0167-4838(94)00053-0

Cited by 39 publications

(18 citation statements)

References 24 publications

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“…A careful literature search failed to identify any cytosolic enzymes that exclusively require free Co2+ for activity, although many examples of enzymes that can be reconstituted with Co2+ and other metals in vitro exist (Bender et al, 1989;Itoh et al, 1994;Yamashiro et al, 1997;Lieder et al, 1998). To the extent that we were able to determine, cytoplasmic enzymes that are active with Co2+ are also active with ZnZ+, Mn2+, and/or Mg2+.…”

Section: Discussionmentioning

confidence: 96%

Yeast methionine aminopeptidase I can utilize either Zn²⁺ or Co²⁺ as a cofactor: A case of mistaken identity?

1998

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Yeast methionine aminopeptidase I (MetAP I) is one of two enzymes in Saccharomyces cerevisiae that is responsible for cotranslational cleavage of initiator methionines. It has previously been classified as a Co2+ metalloprotease in all prokaryotic and eukaryotic forms studied. However, treatment of recombinant apo-MetAP I with 12.5 p M Zn2+ produces an enzyme that is as active as that reconstituted with 200 pM Co2+. In the presence of physiological concentrations of reduced glutathione (GSH), Co-MetAP I is inactive, while the activity of Zn-MetAP I is increased more than 1.7-fold over Zn-MetAP I assayed in the absence of GSH. Given that the in vivo concentration of Zn2+ is at least 1,000-fold higher than that of Co2+, and that Co2+ is insoluble in physiological concentrations of GSH, it is probable that yeast MetAP I is actually a Zn2+ metalloprotease. Furthermore, unless there are extraordinary conditions that insulate or sequester them from this reducing milieu, that have yet to be identified, there are not likely to be any cytoplasmic enzymes that use free Co2+.

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Section: Discussionmentioning

confidence: 96%

Yeast methionine aminopeptidase I can utilize either Zn²⁺ or Co²⁺ as a cofactor: A case of mistaken identity?

1998

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“…The enzyme (M r $ 174,000) is composed of two separable protein moieties, a flavoprotein (FAD-bound, M r $ 120,000) with four identical subunits and a heme protein (M r $ 54,000) with two copies each of two subunits (M r $ 11,500 and 15,500); the complete system is necessary for haloperoxidase activity [8]. NCPO is unusual in requiring the flavoprotein component for peroxidase activity and in having such a small heme subunit size compared to other haloperoxidase enzymes [25][26][27][28].…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic characterization of the ferric states of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase: His-ligated peroxidases with globin-like proximal and distal properties

Osborne

Sumithran

Coggins

et al. 2006

Journal of Inorganic Biochemistry

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“…Bromoperoxidase. Bromoperoxidase from Pseudomonas putida [47], which catalyzes the formation of a carbon–bromine bond in the presence of peroxides, is activated by incubation with cobalt ions but not with other transition metals such as iron, nickel, zinc and vanadate. The enzyme is dimeric, 68 kDa in size and contains cobalt (0.035 nm ± 0.1 mol·mol enzyme –1 ), while bromoperoxidase from the marine red alga Corallina pilulifera contains non‐heme iron, and bromoperoxidase from the fungus Curvularia inaequalis contains zinc and iron.…”

mentioning

confidence: 99%

“…The enzyme is dimeric, 68 kDa in size and contains cobalt (0.035 nm ± 0.1 mol·mol enzyme –1 ), while bromoperoxidase from the marine red alga Corallina pilulifera contains non‐heme iron, and bromoperoxidase from the fungus Curvularia inaequalis contains zinc and iron. The low concentration of cobalt in the P. putida enzyme can be explained by the partial dissociation of cobalt from the enzyme during the purification [47]. Although the enzyme is likely to contain cobalt as an essential metal for bromination [47], further studies are required to elucidate its function.…”

mentioning

confidence: 99%

Cobalt proteins

Kobayashi

Shimizu

1999

European Journal of Biochemistry

416

264

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In the form of vitamin B 12 , cobalt plays a number of crucial roles in many biological functions. However, recent studies have provided information on the biochemistry and bioinorganic chemistry of several proteins containing cobalt in a form other than that in the corrin ring of vitamin B 12 . To date, eight noncorrin-cobalt-containing enzymes (methionine aminopeptidase, prolidase, nitrile hydratase, glucose isomerase, methylmalonyl-CoA carboxytransferase, aldehyde decarbonylase, lysine-2,3-aminomutase, and bromoperoxidase) have been isolated and characterized. A cobalt transporter is involved in the metallocenter biosynthesis of the host cobalt-containing enzyme, nitrile hydratase. Understanding the differences between cobalt and nickel transporters might lead to drug development for gastritis and peptic ulceration.Keywords: cobalt; noncorrin; transporter; metal; inorganic chemistry; methionine aminopeptidase; prolidase; nitrile hydratase; glucose isomerase.Cobalt is a transition metal that occupies a position in the periodic table between iron and nickel. It has two naturally occurring oxidation states (Co 2+ and Co 3+ ), but can exhibit oxidation states from ±I to +IV. This metal is rare in comparison with all known essential trace elements except cadmium and tungsten: 0.0025% (w/w) in the Earth's crust and 4 £ 10 ±8 % (w/v) in sea water. Although cobalt is less frequently encountered in metalloenzymes than the other first-row transition metals (e.g. manganese, iron, copper and zinc), it is nevertheless an important cofactor in vitamin-B 12 -dependent enzymes. Vitamin B 12 [1] contains cobalt in a substituted corrin macrocycle (a porphyrin relative). The B 12 coenzyme possesses an axial Co(III)-alkyl (5 H -deoxyadenosine or methyl) group. Much effort has been concentrated on biochemical studies of this corrin cobalt. In contrast, only a few proteins containing noncorrin cobalt have been characterized.Radioactive cobalt ( 60 Co), which is produced by thermal neutron bombardment of the natural isotope 59 Co, has a half-life of 5.3 years and decays by b-and g-emission to nonradioactive nickel ( 60 Ni). It is used as a concentrated source of g radiation in cancer therapy and food sterilization, and as a radioactive tracer in biological and industrial applications [2]. Because cobalt has characteristic spectra correlated with structural properties (such as observed co-ordination numbers for Co 2+ and Co 3+ ), it has also served as a spectroscopic probe in metalloenzymes. Substituting cobalt for zinc has often been a useful tool to investigate the structural basis of catalytic properties in zinc enzymes and the co-ordination environment of active zinc sites in other proteins [3].Non-corrin cobalt is receiving increased interest not only in bioinorganic chemistry but also in biotechnology, and its availability and remarkable chemical versatility makes cobalt an invaluable catalyst in the chemical industry (e.g. hydroformylation as seen in the oxo process [4]). To date, eight noncorrin-cobalt-containing enzymes hav...

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Purification and characterization of a novel metal-containing nonheme bromoperoxidase from Pseudomonas putida

Cited by 39 publications

References 24 publications

Yeast methionine aminopeptidase I can utilize either Zn²⁺ or Co²⁺ as a cofactor: A case of mistaken identity?

Yeast methionine aminopeptidase I can utilize either Zn²⁺ or Co²⁺ as a cofactor: A case of mistaken identity?

Spectroscopic characterization of the ferric states of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase: His-ligated peroxidases with globin-like proximal and distal properties

Cobalt proteins

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Purification and characterization of a novel metal-containing nonheme bromoperoxidase from Pseudomonas putida

Cited by 39 publications

References 24 publications

Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: A case of mistaken identity?

Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: A case of mistaken identity?

Spectroscopic characterization of the ferric states of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase: His-ligated peroxidases with globin-like proximal and distal properties

Cobalt proteins

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Yeast methionine aminopeptidase I can utilize either Zn²⁺ or Co²⁺ as a cofactor: A case of mistaken identity?

Yeast methionine aminopeptidase I can utilize either Zn²⁺ or Co²⁺ as a cofactor: A case of mistaken identity?