The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)

Stainthorpe, A. C.; Lees, Veronica; Salmond, George P. C.; Dalton, Howard; Murrell, J. Colin

doi:10.1016/0378-1119(90)90158-n

Cited by 169 publications

(141 citation statements)

References 29 publications

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“…The arrangement of the structural genes encoding sMMO in Ms. sporium is similar to those sequenced previously (Cardy et al, 1991b;McDonald et al, 1997;Shigematsu et al, 1999;Stainthorpe et al, 1990). Alignment of the sMMO gene cluster with other sMMO gene clusters clearly demonstrated that Ms. sporium is most closely related to Methylocystis sp.…”

Section: Resultssupporting

confidence: 83%

Duplication of the mmoX gene in Methylosinus sporium: cloning, sequencing and mutational analysis

et al. 2006

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The soluble methane monooxygenase (sMMO) is a key enzyme for methane oxidation, and is found in only some methanotrophs, including Methylosinus sporium 5. sMMO expression is regulated at the level of transcription from a σ 54 promoter by a copper-switch, and is only expressed when the copper-to-biomass ratio during growth is low. Extensive phylogenetic and genetic analyses of sMMOs and other soluble di-iron monooxygenases reveal that these enzymes have only been acquired relatively recently through horizontal gene transfer. In this study, further evidence of horizontal gene transfer was obtained, through cloning and sequencing of the genes encoding the sMMO enzyme complex plus the regulatory genes mmoG and mmoR, and identification of a duplicate copy of the mmoX gene in Ms. sporium. mmoX encodes the α subunit of the hydroxylase of the sMMO enzyme, which constitutes the active site (Prior & Dalton, 1985). The mmoX genes were characterized at the molecular and biochemical levels. Although both copies were transcribed, only mmoX copy 1 was essential for sMMO activity. Construction of an sMMO− mutant by marker-exchange mutagenesis gave some possible insights into the role of the water-soluble pigment in siderophore-mediated iron acquisition. Finally, the amenability of Ms. sporium to genetic manipulation was demonstrated by complementing the sMMO− mutant by heterologous expression of sMMO genes from Methylosinus trichosporium OB3b and Methylococcus capsulatus (Bath), and it was shown that Ms. sporium could be used as an alternative model organism for molecular analysis of MMO regulation.

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Section: Resultssupporting

confidence: 83%

Duplication of the mmoX gene in Methylosinus sporium: cloning, sequencing and mutational analysis

et al. 2006

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“…Among the reductases related to PDR, Gly follows the second Cys ligand in vanillate demethylase reductase (Brunel & Davison, 1988), benzoate dioxygenase reductase (Neidle et al, 1991), and xylene monooxygenase reductase (Suzuki et al, Table 3. 1991). An exception is methane monooxygenase component C, with Ala at the equivalent position (Stainthorpe et al, 1990) and a [2Fe-2S] potential of -220 mV (Lund & Dalton, 1985).…”

Section: The [2fe-2s] Environments In Anabaena Ferredoxin and Pdrmentioning

confidence: 99%

Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin

et al. 1993

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The structure of phthalate dioxygenase reductase (PDR), a monomeric iron-sulfur flavoprotein that delivers electrons from NADH to phthalate dioxygenase, is compared to ferredoxin-NADP+ reductase (FNR) and ferredoxin, the proteins that reduce NADP+ in the final reaction of photosystem I. The folding patterns of the domains that bind flavin, NAD(P), and [2Fe-2S] are very similar in the two systems. Alignment of the X-ray structures of PDR and FNR substantiates the assignment of features that characterize a family of flavoprotein reductases whose members include cytochrome P-450 reductase, sulfite and nitrate reductases, and nitric oxide synthase. Hallmarks of this subfamily of flavoproteins, here termed the FNR family, are an antiparallel 0-barrel that binds the flavin prosthetic group, and a characteristic variant of the classic pyridine nucleotide-binding fold. Despite the similarities between FNR and PDR, attempts to model the structure of a dissociable FNR:ferredoxin complex by analogy with PDR reveal features that are at odds with chemical crosslinking studies (Zanetti, G., Morelli, D., Ronchi, S . , Negri, A., Aliverti, A., & Curti, B., 1988, Biochemistry 27, 3753-3759).Differences in the binding sites for flavin and pyridine nucleotides determine the nucleotide specificities of FNR and PDR. The specificity of FNR for NADP' arises primarily from substitutions in FNR that favor interactions with the 2' phosphate of NADP'. Variations in the conformation and sequences of the loop adjoining the flavin phosphate affect the selectivity for FAD versus FMN.The midpoint potentials for reduction of the flavin and [2Fe-2S] groups in PDR are higher than their counterparts in FNR and spinach ferredoxin, by about 120 mV and 260 mV, respectively. Comparisons of the structure of PDR with spinach FNR and with ferredoxin from Anabaena 7120, along with calculations of electrostatic potentials, suggest that local interactions, including hydrogen bonds, are the dominant contributors to these differences in potential.

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“….... (Taylor, 1988 (Gowri & Campbell, 1989) DMPP-PSEPU = Hydroxylase P5 protein (EC 1.14.13.7) phenol 2-monooxygenase P5 component-Pseudomonas (Nordlund et al, 1990) S15303 = Hypothetical protein 7.6-Salmonella typhimurium (Jiang et al, 1991) MEMC-METCA = Methane monooxygenase component C (EC 1.14.13.25) methane hydroxylase -Methylococcus capsula (Stainthorpe et al, 1990) XYLZ-PSEPU = E 1.2-dioxygenase electron transfer component contains ferredoxin and ferredoxin-NAD(+) (Harayama et al, 1991 (Karplus et al, 1991) amino-terminus was revealed, comprising G[QK] [HFYS] (close to strand S1-5 in Fig. 3).…”

Section: Sequence Alignmentmentioning

confidence: 99%

A structural model for the nucleotide binding domains of the flavocytochrome b_–245 β‐chain

Taylor¹,

1993

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NADPH is a system in phagocytic cells that generates 02-and hydrogen peroxide in the endocytic vacuole, both of which are important for killing of the engulfed microbe. Dysfunction of this oxidase results in the syndrome of chronic granulomatous disease, characterized by a profound predisposition to bacterial and fungal infections. A flavocytochrome b is the site of most of the mutations causing this syndrome. The FAD and NADPH binding sites have been located on the / 3 subunit of this molecule, the C-terminal half of which showed weak sequence similarity to other reductases, including the ferredoxin-NADP reductase (FNR) of known structure. This enabled us to build a model of the nucleotide binding domains of the flavocytochrome using this structure as a template. The model was built initially using a novel automatic modeling method based on distance-matrix projection and then refined using energy minimization with appropriate side-chain torsional constraints. The resulting model rationalized much of the observed sequence conservation and identified a large insertion as a potential regulatory domain. It confirms the inclusion of the neutrophil flavocytochrome b"245 (Cb-245) as a member of the FNR family of reductases and strongly supports its function as the proximal electron transporting component of the NADPH oxidase.

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The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)

Cited by 169 publications

References 29 publications

Duplication of the mmoX gene in Methylosinus sporium: cloning, sequencing and mutational analysis

Duplication of the mmoX gene in Methylosinus sporium: cloning, sequencing and mutational analysis

Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin

A structural model for the nucleotide binding domains of the flavocytochrome b_–245 β‐chain

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The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)

Cited by 169 publications

References 29 publications

Duplication of the mmoX gene in Methylosinus sporium: cloning, sequencing and mutational analysis

Duplication of the mmoX gene in Methylosinus sporium: cloning, sequencing and mutational analysis

Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin

A structural model for the nucleotide binding domains of the flavocytochrome b–245 β‐chain

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A structural model for the nucleotide binding domains of the flavocytochrome b_–245 β‐chain