Premium
Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Struktur des proteinfreien Faktors
Author(s) -
Livingston Douglas A.,
Pfaltz Andreas,
Schreiber Jakob,
Eschnmoser Albert,
AnkelFuchs Dorothe,
Moll Johanna,
Jaenchen Rolf,
Thauer Rudolf K.
Publication year - 1984
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19840670141
Subject(s) - chemistry , stereochemistry , cofactor , hydrolysis , bacteria , enzyme , biochemistry , biology , genetics
Factor F430 from Methanogenic Bacteria: Structure of the Protein‐free Factor Factor F430, the porphinoid nickel‐containing coenzyme of the methylcoenzyme‐M reductase of metanogenic bacteria is shown to be the 3 3 ,8 3 ,12 2 ,13 3 ,18 2 ‐pentaacid derivative of the pentamethylester F430M, the structure of which had been determined previously (see structural formulae 1 and 2 ). The structure assignment rests on chromatographic, UV/VIS‐, CD‐, IR‐, and 13 C‐NMR‐spectroscopic as well as FAB‐mass spectral comparision of F430 with F430M and the pentaacid prepared by acid‐catalyzed hydrolysis of F430M. In the cells of Methanobacterium thermoautotrophicum , factor F430 is present in a ‘bound’ and also, depending on the growth conditions, in ‘free’ form, the latter being defined as the part of total F430 that can be extracted from the cells under extremely mild conditions (80% EtOH at 0–4°). From the (protein)‐‘bound’ form, F430 is extracted by subsequently treating the cells at 0–4° with 80% EtOH containing ( e.g. ), 2m LiCi. From both sources, the extracted factor is the same pentaacid, and there is no indication for the existence of a protein‐free F430 species that would contain additional (covalently bound) structural elements.