Si‐face stereospecificity at C5 of coenzyme F420 for F420‐dependent N5,N10‐methylenetetrahydromethanopterin dehydrogenase, F420‐dependent N5,N10‐methylenetetrahydromethanopterin reductase and F420H2:dimethylnaphthoquinone oxidoreductase

Kunow, Jasper; Schwörer, Beatrix; Setzke, Edgar; Thauer, Rudolf K.

doi:10.1111/j.1432-1033.1993.tb17964.x

Cited by 25 publications

(29 citation statements)

References 43 publications

(47 reference statements)

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“…F,,o is a 5' deazaflavin derivative found in relatively high concentrations in methanogenic archaea (Gorris & van der Drift, 1994). See also the legend to Heterodisulphide reductase (hdrA, hdrBC)++ Schmitz et al (1994) ; Bertram & ; Bertram et al (1994a, b) ; Wasserfallen (1994) ; Hochheimer et al (1995Hochheimer et al ( , 1996; Vorholt et al (1996Vorholt et al ( , 1997b Ermler et al (1997a) ; Kunow et al (1996) 1998) Shima et al (1995 ; Lehmacher Klein et al (1993a) ; Vaupel et al (1996, Klein et al (1993b ; Kunow et al (1993) ;…”

Section: Energy Metabolism Of Methanoarchaeamentioning

confidence: 99%

“…Such an F42oH2 dehydrogenase complex is also found in Archaeoglobus sp. (Kunow et al, 1993(Kunow et al, , 1994Klenk et al, 1997), but is apparently lacking in Methanococcus spp. (Bult et al, 1996) and Methanobacterium sp.…”

Section: Heterodisulphide Reduction With F42a2mentioning

confidence: 99%

“…Klein & Thauer ( , 1997 ; Mukhopadhyay et al (1995Mukhopadhyay et al ( ) (1994Mukhopadhyay et al ( , 1995 ; Klein et al (1995a, b) ; Berkessel & ; Hartmann et al (1996a, b);Thauer et al (1996) (1995a) ; Kunow et al (1993) Schworer et al (1993b) ; Schleucher et al…”

Section: R K T H a U E Rmentioning

confidence: 99%

“…HdrE is a b-type cytochrome (Kiinkel et al, 1997(Kiinkel et al, , 1998. (Schworer et al, 1993a;Kunow et al, 1993Kunow et al, ,1994Vorholt et al, 1995Vorholt et al, , 1997a.…”

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Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

1998

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Historical overview In 1933, Stephenson & Stickland (1933a) published that they had isolated from river mud, by the single cell technique, a methanogenic organism capable of growth in an inorganic medium with formate as the sole carbon source. 4 H C 0 0-+ 4H' + CH, + 3 C 0 , + 2H,O AGO' =-144-5 kJ mol-' Methane formation from formate was shown to occur in a stepwise manner, by the preliminary decomposition of formic acid into CO, and H, followed by a reduction of CO, by H,, suggesting that formate was not an intermediate in the reduction of CO, to methane. HCOO-+ H+-+ H, + CO, 4H,+CO,-+ C H , + 2 H 2 0 AGO' =-3-5 kJ mol-' AGO' =-131 kJ mol-' Cell suspensions of the microorganism catalysed the reduction of methylene blue with H,, indicating that the methanogen contained an enzyme which activates molecular hydrogen. H,-+ 2e-+ 2H+ E; =-414mV This enzyme had been discovered by Stephenson & Stickland (1931a) 2 years before in a number of bacterial species and was named by them 'hydrogenase'. The paper by Stephenson & Stickland (1933a) is considered to mark the beginning of the modern era for study of methanogenesis (Wolfe, 1993). It is the first Except when otherwise noted, the free energy changes given for methanogenic reactions were calculated from the free energies of formation from the elements of the substrates and products with non-gaseous compounds at 1 M aqueous solution and gaseous compounds in the gaseous state at 1 atmosphere pressure (101 kPa). The free energy changes of formation were taken from Thauer eta/. (1977). 0002-2667 0 1998 SGM Glucose-+ 3C0, + 3CH, AGO' =-418.1 kJ mol-' This reaction is not catalysed by single microorganisms but by syntrophic associations of microorganisms. First the glucose is fermented to acetate, CO, and H, or to acetate, formate and H, : Glucose + 2H,O + 2CH3COO-+ 2H' + 2C0, + 4H2 AGO' =-215.7 kJ mol-' Glucose + 2H20-+ 2CH3COO-+ 2HC00-+ 4H' + 2H, AGO' =-208.7 kJ mol-1 These fermentations are brought about by strictly anaerobic bacteria and/or protozoa. In a second step, the products of glucose fermentation are then converted to methane, the rate of conversion being such that the concentrations of acetate (< 1 mM), formate (< 0.1 mM) and H, (< 1 pM) in the anaerobic sediments remain very low (Zinder, 1993). CH3COO-+Hf-+ C02+CH, AGO' =-36 kJ mol-' 4H, + CO,-+ CH, + 2H20 AGO' =-131 kJ mol-' 4HC00-+4H+ + CH,+3C02+2H,0 AGO' =-144.5 kJ mol-' H-S-CoM, coenzyme M ; H-S-COB, coenzyme B ; H,SPT, tetrahydrosarcinapterin, which is the modified tetrahydromethanopterin (for structures see Fig. 3) present in the Methanosarcinales (Gorris & van der Drift, 1994). Reaction" Enzyme (gene) Most recent literature Acetate + CoA + acetyl-CoA + H,O AGO' = + 35.7 k J rnol-lt

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Section: Energy Metabolism Of Methanoarchaeamentioning

confidence: 99%

Section: Heterodisulphide Reduction With F42a2mentioning

confidence: 99%

Section: R K T H a U E Rmentioning

confidence: 99%

“…HdrE is a b-type cytochrome (Kiinkel et al, 1997(Kiinkel et al, , 1998. (Schworer et al, 1993a;Kunow et al, 1993Kunow et al, ,1994Vorholt et al, 1995Vorholt et al, , 1997a.…”

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Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

1998

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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

152

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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Structure of Coenzyme F420 Dependent Methylenetetrahydromethanopterin Reductase from Two Methanogenic Archaea

Shima

Warkentin

Grabarse

et al. 2000

Journal of Molecular Biology

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Si‐face stereospecificity at C5 of coenzyme F₄₂₀ for F₄₂₀‐dependent N⁵,N¹⁰‐methylenetetrahydromethanopterin dehydrogenase, F₄₂₀‐dependent N⁵,N¹⁰‐methylenetetrahydromethanopterin reductase and F₄₂₀H₂:dimethylnaphthoquinone oxidoreductase

Cited by 25 publications

References 43 publications

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

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

Structure of Coenzyme F420 Dependent Methylenetetrahydromethanopterin Reductase from Two Methanogenic Archaea

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Si‐face stereospecificity at C5 of coenzyme F420 for F420‐dependent N5,N10‐methylenetetrahydromethanopterin dehydrogenase, F420‐dependent N5,N10‐methylenetetrahydromethanopterin reductase and F420H2:dimethylnaphthoquinone oxidoreductase

Cited by 25 publications

References 43 publications

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

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

Structure of Coenzyme F420 Dependent Methylenetetrahydromethanopterin Reductase from Two Methanogenic Archaea

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Resources

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Si‐face stereospecificity at C5 of coenzyme F₄₂₀ for F₄₂₀‐dependent N⁵,N¹⁰‐methylenetetrahydromethanopterin dehydrogenase, F₄₂₀‐dependent N⁵,N¹⁰‐methylenetetrahydromethanopterin reductase and F₄₂₀H₂:dimethylnaphthoquinone oxidoreductase

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