In:
European Journal of Biochemistry, Wiley, Vol. 170, No. 1-2 ( 1987-12), p. 459-467
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1987.170.issue-1-2
DOI:
10.1111/j.1432-1033.1987.tb13722.x
Language:
English
Publisher:
Wiley
Publication Date:
1987
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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