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Interconversion of F430derivatives of methanogenic bacteria

✍ Scribed by J. T. Keltjens; J. M. H. Hermans; G. J. F. A. Rijsdijk; C. Drift; G. D. Vogels


Book ID
104776522
Publisher
Springer Netherlands
Year
1988
Tongue
English
Weight
682 KB
Volume
54
Category
Article
ISSN
0003-6072

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✦ Synopsis


F430 is the prosthetic group of the methylcoenzyme M reductase of methanogenic bacteria. The compound isolated from Methanosarcina barkeri appears to be identical to the one obtained from the only distinctly related Methanobacterium thermoautotrophicum. F430 is thermolabile and in the presence of acetonitrile or C104 two epimerization products are obtained upon heating; in the absence of these compounds F430 is oxidized to 12, 13-didehydro-F430. The latter is stereoselectively reduced under Hz atmosphere to F430 by cell-free extracts of M. barkeri or M. thermoautotrophicum. H2 may be replaced by the reduced methanogenic electron carrier coenzyme F420.

Abbreviations: CH3S-CoM -methylcoenzyme M, 2-methylthioethanesulfonic acid; HS-CoMcoenzyme M, 2-mercaptoethanesulfonic acid; F430 -Ni(II) tetrahydro-(1213, 13a)-corphin with a uroporphinoid (III) ligand skeleton; 13-epi-F430 and 12,13-di-epi-F430 -the 1213, 1313-and 12c~, 1313-derivatives of 17430; 12, 13-didehydro-F430 -F430 oxidized at C-12 and C-13; coenzyme F420 -7,8-didemethyl-8-hydroxy-5-deazaflavin derivative; coenzyme F4z0H2-reduced coenzyme F420; MV Γ· -methylviologen semiquinone; HPLC -high-performance liquid chromatography.


πŸ“œ SIMILAR VOLUMES


Coenzyme F430 from Methanogenic Bacteria
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1. Introduction. the hydrocorphinoid nickel complex 1 (F430) [l] is the cofactor of methyl-coenzyme M reductase which catalyzes the last step of methane formation in methanogenic bacteria according to Scheme l a . The mechanism by which the enzyme

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Coenzyme F42o is a 8-hydroxy-5-deazaflavin present in methanogenic bacteria. We have investigated whether the pyrimidine ring of the deazaflavin originates from guanine as in flavin biosynthesis, in which the pyrimidine ring of guanine is conserved. For this purpose the incorporation of [2-14C]guani