Cytochrome c peroxidase from Methylococcus capsulatus Bath

Zahn, James A.; Arciero, David M.; Hooper, Alan B.; Coats, Joel R.; DiSpirito, Alan A.

doi:10.1007/s002030050510

Cited by 49 publications

(58 citation statements)

References 32 publications

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“…Thus, it is tempting to speculate that these proteins have an equivalent role in methanotrophs in the formation of kynurenine, by carrying out appropriate electron-transfer reactions. On the other hand, methylamine dehydrogenase activity is not detected in M. capsulatus (Zahn et al, 1997), and homologues of the genes in the mau gene cluster involved in methylamine dehydrogenase activity are not found in the M. capsulatus genome (Ward et al, 2004). It is therefore unlikely that MopE/SACCP proteins are involved in methylamine dehydrogenase activity and thus, by inference, neither are CorA/CorB in M. album BG8.…”

Section: Discussionmentioning

confidence: 92%

Identification of a bacterial di-haem cytochrome c peroxidase from Methylomicrobium album BG8

2010

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The nucleotide sequence of an open reading frame (corB) downstream of the copper-repressible CorA-encoding gene of the methanotrophic bacterium Methylomicrobium album BG8 was obtained by restriction enzyme digestion and inverse PCR. The amino acid sequence deduced from this gene showed significant sequence similarity to the surface-associated di-haem cytochrome c peroxidase (SACCP) previously isolated from Methylococcus capsulatus (Bath), including both c-type haem-binding motifs. Homology analysis placed this protein, phylogenetically, within the subfamily containing the M. capsulatus SACCP of the bacterial dihaem cytochrome c peroxidase (BCCP) family of proteins. Immunospecific recognition confirmed synthesis of the M. album CorB as a protein non-covalently associated with the outer membrane and exposed to the periplasm. corB expression is regulated by the availability of copper ions during growth and the protein is most abundant in M. album when grown at a low copper-tobiomass ratio, indicating an important physiological role of CorB under these growth conditions. corB was co-transcribed with the gene encoding CorA, constituting a copper-responding operon, which appears to be under the control of a s 54 -dependent promoter. M. album CorB is the second isolated member of the recently described subfamily of the BCCP family of proteins. So far, these proteins have only been described in methanotrophic bacteria. INTRODUCTIONA surface-associated cytochrome c peroxidase (SACCP) isolated from the methanotrophic bacterium Methylococcus capsulatus (Bath) has recently been described (Karlsen et al., 2005). This protein shares significant sequence similarity with the members of the bacterial di-haem cytochrome c peroxidase family of proteins (BCCP, pfam03150) and appears to have a core structure resembling the resolved structures available from this family (Karlsen et al., 2005). However, the M. capsulatus SACCP can be distinguished from the other members of the BCCP family by being a much larger protein when compared to both the di-haem cytochrome c peroxidases and the MauG proteins, which constitute the two subfamilies (Chistoserdov et al., 1994;Ronnberg & Ellfolk, 1979). Furthermore, the two c-type haem-binding motifs of the M. capsulatus SACCP have, in their primary sequence, an increased inter-haem distance.However, structural analyses (Karlsen et al., 2005) strongly suggests that these haem groups in the native protein are structurally located in close proximity to each other, as previously demonstrated for other di-haem cytochrome c peroxidases (Fulop et al., 1995;Shimizu et al., 2001). We have suggested that the M. capsulatus SACCP protein is included in a third, novel subfamily of the BCCP family of proteins (Karlsen et al., 2005). In contrast to the di-haem cytochrome c peroxidases and the MauGs, which are localized in the periplasm (Goodhew et al., 1990; Wang et al., 2003), the M. capsulatus SACCP was isolated from the bacterial cell surface (Karlsen et al., 2005). Copperregulated multiple c-type cytochrom...

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Section: Discussionmentioning

confidence: 92%

Identification of a bacterial di-haem cytochrome c peroxidase from Methylomicrobium album BG8

2010

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“…The derived amino acid sequence showed high similarity values to cytochrome c peroxidases from P. aeroginosa, Helicobacter spp., and Aquifex spp. Zahn et al (35) purified a cytochrome c peroxidase from M. capsulatus Bath. They discussed its possible importance in detoxification, as the monooxygenase mechanism involves the activation of oxygen.…”

Section: Discussionmentioning

confidence: 99%

Molecular Analysis of the pmo (Particulate Methane Monooxygenase) Operons from Two Type II Methanotrophs

Gilbert

McDonald

Finch

et al. 2000

Appl Environ Microbiol

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The particulate methane monooxygenase gene clusters, pmoCAB, from two representative type II methanotrophs of the ␣-Proteobacteria, Methylosinus trichosporium OB3b and Methylocystis sp. strain M, have been cloned and sequenced. Primer extension experiments revealed that the pmo cluster is probably transcribed from a single transcriptional start site located 300 bp upstream of the start of the first gene, pmoC, for Methylocystis sp. strain M. Immediately upstream of the putative start site, consensus sequences for 70 promoters were identified, suggesting that these pmo genes are recognized by 70 and negatively regulated under low-copper conditions. The pmo genes were cloned in several overlapping fragments, since parts of these genes appeared to be toxic to the Escherichia coli host. Methanotrophs contain two virtually identical copies of pmo genes, and it was necessary to use Southern blotting and probing with pmo gene fragments in order to differentiate between the two pmoCAB clusters in both methanotrophs. The complete DNA sequence of one copy of pmo genes from each organism is reported here. The gene sequences are 84% similar to each other and 75% similar to that of a type I methanotroph of the ␥-Proteobacteria, Methylococcus capsulatus Bath. The derived proteins PmoC and PmoA are predicted to be highly hydrophobic and consist mainly of transmembranespanning regions, whereas PmoB has only two putative transmembrane-spanning helices. Hybridization experiments showed that there are two copies of pmoC in both M. trichosporium OB3b and Methylocystis sp. strain M, and not three copies as found in M. capsulatus Bath.Methane-oxidizing bacteria (methanotrophs) play an important part in the global carbon cycle, recycling up to 60% (680 Tg) of total global methane production per year (25). Methane is used as the sole source of carbon and energy by these organisms. It is oxidized to methanol by the key enzyme methane monooxygenase (MMO). Methanol is further oxidized to formaldehyde. Formaldehyde is then either assimilated into cell biomass or oxidized via formate to carbon dioxide. All known methanotrophs possess the membrane-bound or particulate form of MMO (pMMO), and some have a second enzyme, the cytoplasmic, or soluble, MMO (sMMO).Two types of methanotrophs can be distinguished on the basis of biochemical and ultrastructural differences (3, 33). Genetic and biochemical work has been carried out mainly on two organisms, the type I methanotroph Methylococcus capsulatus Bath, a ␥-proteobacterium, and the type II methanotroph Methylosinus trichosporium OB3b, an ␣-proteobacterium. Another well-studied type II organism, Methylocystis sp. strain M, was isolated from a trichloroethylene-degrading mixed culture (20, 32). The sMMOs of these bacteria are very similar (5, 10, 20), and their sMMO gene sequences are highly conserved (17).Recently, the pMMO was purified from M. capsulatus Bath (21, 34) and M. trichosporium OB3b (31). It is a copper-containing monooxygenase which is oxygen and light sensitive. The 26-kDa subunit o...

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“…Cell lysis and initial separation of methanol dehydrogenase from soluble c-type cytochromes were preformed as described by Bergmann et al (7) and Zahn et al (53).…”

Section: Methodsmentioning

confidence: 99%

“…An evaluation of fractions from the Resource Q column showed that at least three redox-active proteins were separated from formaldehyde dehydrogenase at this step: cytochrome b 559/569 complex (54), a monoheme cytochrome c 553 (53), and cytochrome c 556 peroxidase (53). As isolated, cytochrome b 559/569 complex appears to be the cytochrome bc 1 complex in M. capsulatus Bath minus the c-type cytochrome and the Rieske iron-sulfur protein.…”

Section: Dl-faldh Contains Sequence Motifs For Zinc As Well As Nad(p)mentioning

confidence: 99%

Membrane-Associated Quinoprotein Formaldehyde Dehydrogenase from Methylococcus capsulatus Bath

et al. 2001

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Cytochrome c peroxidase from Methylococcus capsulatus Bath

Cited by 49 publications

References 32 publications

Identification of a bacterial di-haem cytochrome c peroxidase from Methylomicrobium album BG8

Identification of a bacterial di-haem cytochrome c peroxidase from Methylomicrobium album BG8

Molecular Analysis of the pmo (Particulate Methane Monooxygenase) Operons from Two Type II Methanotrophs

Membrane-Associated Quinoprotein Formaldehyde Dehydrogenase from Methylococcus capsulatus Bath

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