Isolation and structural identification of a chromophoric coenzyme F420 fragment from culture fluid of Methanobacterium thermoautotrophicum

1983 ◽  
Vol 136 (3) ◽  
pp. 191-193 ◽  
Author(s):  
Rainer Kern ◽  
Paul J. Keller ◽  
Gerhard Schmidt ◽  
Adelbert Bacher
Keyword(s):  
Culture Fluid ◽  
Structural Identification ◽  
Methanobacterium Thermoautotrophicum ◽  
Coenzyme F420

Biosynthesis of coenzyme F420 and methanopterin in Methanobacterium thermoautotrophicum

1990 ◽  
Vol 153 (3) ◽  
pp. 259-263 ◽  
Author(s):  
Bruno Schwarzkopf ◽  
Brigitte Reuke ◽  
Andreas Kiener ◽  
Adelbert Bacher
Keyword(s):  
Methanobacterium Thermoautotrophicum ◽  
Coenzyme F420

scholarly journals Function of Coenzyme F420 in Aerobic Catabolism of 2,4,6-Trinitrophenol and 2,4-Dinitrophenol by Nocardioides simplex FJ2-1A

1999 ◽  
Vol 181 (9) ◽  
pp. 2669-2674 ◽  
Author(s):  
Sybille Ebert ◽  
Paul-Gerhard Rieger ◽  
Hans-Joachim Knackmuss
Keyword(s):  
Aromatic Compounds ◽  
Enzyme System ◽  
Picric Acid ◽  
Methanobacterium Thermoautotrophicum ◽  
Bacterial Degradation ◽  
Coenzyme F420 ◽  
Terminal Sequence ◽  
Aromatic System ◽  
Two Component ◽  
Protein Components

ABSTRACT 2,4,6-Trinitrophenol (picric acid) and 2,4-dinitrophenol were readily biodegraded by the strain Nocardioides simplexFJ2-1A. Aerobic bacterial degradation of these π-electron-deficient aromatic compounds is initiated by hydrogenation at the aromatic ring. A two-component enzyme system was identified which catalyzes hydride transfer to picric acid and 2,4-dinitrophenol. Enzymatic activity was dependent on NADPH and coenzyme F420. The latter could be replaced by an authentic preparation of coenzyme F420 fromMethanobacterium thermoautotrophicum. One of the protein components functions as a NADPH-dependent F420 reductase. A second component is a hydride transferase which transfers hydride from reduced coenzyme F420 to the aromatic system of the nitrophenols. The N-terminal sequence of the F420 reductase showed high homology with an F420-dependent NADP reductase found in archaea. In contrast, no N-terminal similarity to any known protein was found for the hydride-transferring enzyme.

Purification and characterization of coenzyme F420-dependent 5,10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum strain ΔH

1991 ◽  
Vol 1073 (1) ◽  
pp. 77-84 ◽  
Author(s):  
B.W. te Brömmelstroet ◽  
Charles M.H. Hensgens ◽  
Jan T. Keltjens ◽  
Chris van der Drift ◽  
Godfried D. Vogels
Keyword(s):  
Methanobacterium Thermoautotrophicum ◽  
Coenzyme F420 ◽  
Purification And Characterization

Hydrogen-forming and coenzyme-F420-reducing methylene tetrahydromethanopterin dehydrogenase are genetically distinct enzymes in Methanobacterium thermoautotrophicum (Marburg)

1991 ◽  
Vol 202 (3) ◽  
pp. 1205-1208 ◽  
Author(s):  
Rudolf BUNAU ◽  
Carmen ZIRNGIBL ◽  
Rudolf K. THAUER ◽  
Albrecht KLEIN
Keyword(s):  
Methanobacterium Thermoautotrophicum ◽  
Coenzyme F420

scholarly journals Methanococcus jannaschii Coenzyme F420 Analogs Contain a Terminal α-Linked Glutamate

2003 ◽  
Vol 185 (15) ◽  
pp. 4662-4665 ◽  
Author(s):  
Marion Graupner ◽  
Robert H. White
Keyword(s):  
Mycobacterium Smegmatis ◽  
Methanobacterium Thermoautotrophicum ◽  
Methanosarcina Barkeri ◽  
Archaeoglobus Fulgidus ◽  
Methanococcus Jannaschii ◽  
Coenzyme F420 ◽  
Methanosarcina Thermophila ◽  
Predominant Form

ABSTRACT Analyses of the F420s present in Methanococcus jannaschii have shown that these cells contain a series of γ-glutamyl-linked F420s capped with a single, terminal α-linked l-glutamate. The predominant form of F420 was designated as α-F420-3 and represented 86% of the F420s in these cells. Analyses of Methanosarcina thermophila, Methanosarcina barkeri, Methanobacterium thermoautotrophicum, Archaeoglobus fulgidus, and Mycobacterium smegmatis showed that they contained only γ-glutamyl-linked F420s.

scholarly journals Large-Scale Production of Coenzyme F420-5,6 by Using Mycobacterium smegmatis

2002 ◽  
Vol 68 (11) ◽  
pp. 5750-5755 ◽  
Author(s):  
Dale Isabelle ◽  
D. Randall Simpson ◽  
Lacy Daniels
Keyword(s):  
Ion Exchange ◽  
Mycobacterium Smegmatis ◽  
Large Scale ◽  
Methanobacterium Thermoautotrophicum ◽  
Scale Production ◽  
Coenzyme F420 ◽  
Biosynthetic Precursor ◽  
Large Scale Production ◽  
Exchange Material ◽  
Aerobic Actinomycetes

ABSTRACT Production of coenzyme F420 and its biosynthetic precursor FO was examined with a variety of aerobic actinomycetes to identify an improved source for these materials. Based on fermentation costs, safety, and ease of growth, Mycobacterium smegmatis was the best source for F420-5,6. M. smegmatis produced 1 to 3 μmol of intracellular F420 per liter of culture, which was more than the 0.85 to 1.0 μmol of F420-2 per liter usually obtained with Methanobacterium thermoautotrophicum and ∼10-fold higher than what was previously reported for the best aerobic actinomycetes. An improved chromatography system using rapidly flowing quaternary aminoethyl ion-exchange material and Florisil was used to more quickly and easily purify F420 than with previous methods.

scholarly journals Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain delta H.

1990 ◽  
Vol 265 (4) ◽  
pp. 1852-1857
Author(s):  
B W te Brömmelstroet ◽  
C M Hensgens ◽  
J T Keltjens ◽  
C van der Drift ◽  
G D Vogels
Keyword(s):  
Methanobacterium Thermoautotrophicum ◽  
Coenzyme F420 ◽  
Purification And Properties
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