An improved method for separating analogues of coenzyme F420 by isocratic reversed-phase high performance liquid chromatography is described. The method offers improved resolution, shorter chromatography runs and requires less complex apparatus.
Studies on the biosynthesis of coenzyme F420in methanogenic bacteria
✍ Scribed by Rolf Jaenchen; Peter Schönheit; Rudolf K. Thauer
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 420 KB
- Volume
- 137
- Category
- Article
- ISSN
- 0302-8933
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✦ Synopsis
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]guanine and of [8-14C]guanine into F4zo by growing cultures of Methanobacterium thermoautotrophicum was studied. Only in the case of [2-14C]guanine did F~z0 become labeled. The specific radioactivity of the deazaflavin and of guanine isolated from nucleic acids of [2-~4C]guanine grown cells were identical. This finding suggests that the pyrimidine ring of the deazaflavin and of flavins are synthesized by the same pathway.
F4z0 did not become labeled when M. thermoauto- trophicum was grown in the presence of methyl-[~4C] methionine, [U-14C]phenylalanine or [U-14C]tyrosine. This excludes that C-5 of the deazaflavin is derived from the methyl group ofmethionine and that the benzene ring comes from phenylalanine or tyrosine.
📜 SIMILAR VOLUMES
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
## ~ ~~ F430M, the pentamethyl ester of coenzyme F430, can be oxidized reversibly by one electron. The oxidation potential has been determined, and the electrolytically prepared oxidation product was characterized by its UVjVIS and ESR spectrum. The strongly anisotropic and nearly axial ESR spectr