Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri

Bw, te Brömmelstroet; Wj, Geerts; Jt, Keltjens; C, van der Drift; Gd, Vogels

doi:10.1016/0167-4838(91)90072-8

Cited by 35 publications

(14 citation statements)

References 26 publications

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“…The reductase of Methanosarcina strain Gol is a soluble protein, which is in agreement with findings on the corresponding enzyme from Methanosarcina barkeri and Methanobacterium thermoautotrophicum (15,16,25). The methyltransferase of Methanosarcina strain Gol, however, is a membrane protein, and its activity is Na+ dependent.…”

Section: Discussionsupporting

confidence: 78%

“…There is no evidence for such a membrane association of methylene-H4MPT reductase. This enzyme was purified from the soluble fraction of cell extracts of several methanogenic bacteria (15,16,25). Its localization in the cytoplasm and the reversibility of the reaction catalyzed, as well as the low AG0' value of the reaction, were taken as an indication against a possible function in energy conservation (26).…”

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confidence: 99%

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N5-methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina strain Gö1 is an Na(+)-translocating membrane protein

1992

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To determine the cellular localization of components of the methyltransferase system, we separated cell extracts of Methanosarcina strain Gol into cytoplasmic and inverted-vesicle fractions. Measurements demonstrated that 83% of the methylene-tetrahydromethanopterin reductase activity resided in the cytoplasm whereas 88% of the methyl-tetrahydromethanopterin:coenzyme M methyltransferase (methyltransferase) was associated with the vesicles. The activity of the methyltransferase was stimulated 4.6-fold by ATP and 10-fold by ATP plus a reducing agent [e.g., Ti(III)J. In addition, methyltransferase activity depended on the presence of Na+ (apparent Km = 0.7 mM) and Na+ was pumped into the lumen of the vesicles in the course of methyl transfer from methyl-tetrahydromethanopterin not only to coenzyme M but also to hydroxycobalamin. Both methyl transfer reactions were inhibited by 1-iodopropane and reconstituted by illumination. A model for the methyl transfer reactions is presented.

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Section: Discussionsupporting

confidence: 78%

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confidence: 99%

N5-methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina strain Gö1 is an Na(+)-translocating membrane protein

1992

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“…11) (166). The reaction is catalyzed through a ternary complex mechanism (276,284), wherein hydride transfer occurs between C-14a of methylene-H 4 MPT (Re-face stereospecific) and C-5 of F 420 H 2 (Si-face stereospecific) (166, [287][288][289]. Crystal structures of Mer homologs have been solved from three organisms, Methanoplanus kandleri (159), Methanothermobacter marburgensis (159), and Methanosarcina barkeri (48).…”

Section: Adf: F 420 -Reducing Secondary Alcohol Dehydrogenasementioning

confidence: 99%

Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions

Greening

Ahmed

Mohamed

et al. 2016

Microbiol Mol Biol Rev

159

208

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SUMMARY5-Deazaflavin cofactors enhance the metabolic flexibility of microorganisms by catalyzing a wide range of challenging enzymatic redox reactions. While structurally similar to riboflavin, 5-deazaflavins have distinctive and biologically useful electrochemical and photochemical properties as a result of the substitution of N-5 of the isoalloxazine ring for a carbon. 8-Hydroxy-5-deazaflavin (Fo) appears to be used for a single function: as a light-harvesting chromophore for DNA photolyases across the three domains of life. In contrast, its oligoglutamyl derivative F420is a taxonomically restricted but functionally versatile cofactor that facilitates many low-potential two-electron redox reactions. It serves as an essential catabolic cofactor in methanogenic, sulfate-reducing, and likely methanotrophic archaea. It also transforms a wide range of exogenous substrates and endogenous metabolites in aerobic actinobacteria, for example mycobacteria and streptomycetes. In this review, we discuss the physiological roles of F420in microorganisms and the biochemistry of the various oxidoreductases that mediate these roles. Particular focus is placed on the central roles of F420in methanogenic archaea in processes such as substrate oxidation, C1pathways, respiration, and oxygen detoxification. We also describe how two F420-dependent oxidoreductase superfamilies mediate many environmentally and medically important reactions in bacteria, including biosynthesis of tetracycline and pyrrolobenzodiazepine antibiotics by streptomycetes, activation of the prodrugs pretomanid and delamanid byMycobacterium tuberculosis, and degradation of environmental contaminants such as picrate, aflatoxin, and malachite green. The biosynthesis pathways of Foand F420are also detailed. We conclude by considering opportunities to exploit deazaflavin-dependent processes in tuberculosis treatment, methane mitigation, bioremediation, and industrial biocatalysis.

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“…The two substrates are interchangeable in enzyme assays. Methylene-H 4 SPT dehydrogenase (Mtd) was assayed by following the formation of methenyl-H 4 MPT from methylene-H 4 MPT with F 420 as electron acceptor (27). Methenyl-H 4 SPT cyclohydrolase (Mch) was assayed according to ref.…”

Section: Formation Of Co2 and H2 From Cho-mfr By Membrane Fractionsmentioning

confidence: 99%

Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation

Meuer

Kuettner

Zhang

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

166

174

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(ii) Under autotrophic growth conditions, the enzyme catalyzes the energetically unfavorable reduction of ferredoxin by H 2, most probably driven by reversed electron transport, and the reduced ferredoxin thus generated functions as low potential electron donor for the synthesis of pyruvate in an anabolic pathway. (iii) Reduced ferredoxin in addition provides the reducing equivalents for the first step of methanogenesis from H 2͞CO2, the reduction of CO2 to formylmethanofuran. Thus, in vivo genetic analysis has led to the identification of the electron donor of this key initial step of methanogenesis.

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Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri

Cited by 35 publications

References 26 publications

N5-methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina strain Gö1 is an Na(+)-translocating membrane protein

N5-methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina strain Gö1 is an Na(+)-translocating membrane protein

Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions

Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation

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Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri

Cited by 35 publications

References 26 publications

N5-methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina strain Gö1 is an Na(+)-translocating membrane protein

N5-methyl-tetrahydromethanopterin:coenzyme M methyltransferase of Methanosarcina strain Gö1 is an Na(+)-translocating membrane protein

Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions

Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation

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Physiology, Biochemistry, and Applications of F₄₂₀- and F_o-Dependent Redox Reactions