Open AccessBiosynthesis of coenzyme F430 in methanogenic bacteria
Author(s) -
PFALTZ Andreas,
KOBELT André,
HÜSTER Rudolf,
THAUER Rudolf K.
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13722.x
Subject(s) - bacteria , biosynthesis , enzyme , cofactor , chemistry , stereochemistry , biochemistry , methanogenesis , nickel , methane , biology , organic chemistry , genetics
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 14 C‐labelling experiments, fast‐atom‐bombardment mass spectra, 1 H‐NMR spectra of the corresponding hexamethyl ester, and ultraviolet/visible spectral comparison with model compounds. In cell extracts and in intact cells of methanogenic bactera, 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.