Biosynthesis of coenzyme F430 in methanogenic bacteria. Identification of 15,17(3)-seco-F430-17(3)-acid as an intermediate.
Coenzyme F430 is a hydroporphinoid nickel complex present in all methanogenic bacteria. It is part of the enzyme system which catalyzes methane formation from methyl-coenzyme M. We describe here that under certain conditions a second nickel porphinoid accumulates in methanogenic bacteria. The compound was identified at 15,17(3)-seco-F430-17(3)-acid. The structural assignment rests on 14C-labelling experiments, fast-atom-bombardment mass spectra, 1H-NMR spectra of the corresponding hexamethyl ester, and ultraviolet/visible spectral comparison with model compounds. In cell extracts and in intact cells of methanogenic bacteria, 15,17(3)-seco-F430-17(3)-acid was converted to F430. These findings indicate that the new nickel-containing porphinoid is an intermediate in the biosynthesis of coenzyme F430.
Laboratorium für Organische Chemie, Eidgenössische Technische Hochschule, Zürich, Federal Republic of Germany.
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Pfaltz
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Kobelt
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Hüster
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RK
Thauer
D003067:Coenzymes / Q000096:biosynthesis*; D019605:Euryarchaeota / Q000254:growth & development / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008665:Metalloporphyrins; D008667:Metalloproteins / Q000096:biosynthesis* / Q000302:isolation & purification; D009532:Nickel / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism*; D013045:Species Specificity; D013053:Spectrophotometry
D003067:Coenzymes; D008665:Metalloporphyrins; D008667:Metalloproteins; C023540:factor F430; D009532:Nickel