Chapter 4 Biochemistry of coenzyme F430, a nickel porphinoid involved in methanogenesis
- 1 January 1991
- book chapter
- Published by Elsevier
Abstract
No abstract availableThis publication has 78 references indexed in Scilit:
- Methanobacterium thermoautotrophicum contains a soluble enzyme system that specifically catalyzes the reduction of the heterodisulfide of coenzyme M and 7‐mercaptoheptanoylthreonine phosphate with H2FEBS Letters, 1988
- Five new EPR signals assigned to nickel in methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum, strain MarburgBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Coenzyme F430 from methanogenic bacteria: methane formation by reductive carbon–sulphur bond cleavage of methyl sulphonium ions catalysed by F430 pentamethyl esterJournal of the Chemical Society, Chemical Communications, 1988
- Ribonuclease‐sensitive δ‐aminolevulinic acid formation from glutamate in cell extracts of Methanobacterium thermoautotrophicumFEBS Letters, 1986
- Sirohydrochlorin, a precursor of factor F430 biosynthesis in Methanobacterium thermoautotrophicumFEBS Letters, 1985
- Determination of the crystal structure of a petroporphyrin isolated from oil shaleNature, 1983
- Presence of coenzyme M derivatives in the prosthetic group (coenzyme MF430) of methylcoenzyme M reductase from Methanobacterium thermoautotrophicumBiochemical and Biophysical Research Communications, 1982
- Incorporation of methionine‐derived methyl groups into factor F430 by Methanobacterium thermoautotrophicumFEBS Letters, 1981
- Biosynthetic evidence for a nickel tetrapyrrole structure of factor F430 from Methanobacterium thermoautotrophicumFEBS Letters, 1980
- Presence of nickel in Factor F430 from MethanobacteriumbryantiiBiochemical and Biophysical Research Communications, 1980