Methane as the product of reaction of methyl-coenzyme-M with monovalent nickel complexes in aqueous solutions. A model for the in vivo activity of cofactor F430
Author:
Publisher
Elsevier BV
Subject
Materials Chemistry,Inorganic Chemistry,Physical and Theoretical Chemistry
Reference24 articles.
1. Metal Ions in Biological Systems;Sigel,1988
2. Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Struktur des proteinfreien Faktors
3. Coenzyme F430 from Methanogenic Bacteria: Complete Assignment of Configuration Based on an X-Ray Analysis of 12,13-Diepi-F430 Pentamethyl Ester and on NMR Spectroscopy
4. Bending of the reduced porphyrin of factor F430 can accommodate a trigonal-bipyramidal geometry at nickel: a conformational analysis of this nickel-containing tetrapyrrole, in relation to archaebacterial methanogenesis
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1. Model Studies of Methyl CoM Reductase: Methane Formation via CH3–S Bond Cleavage of Ni(I) Tetraazacyclic Complexes Having Intramolecular Methyl Sulfide Pendants;Inorganic Chemistry;2012-03-22
2. Coordination of Coenzyme M and Its Derivatives on Ni II (tetraazacycle) Complexes: A Model for the Active Site of Methyl Coenzyme M Reductase;European Journal of Inorganic Chemistry;2010-09-15
3. Metil coenzima M redutase (MCR) e o fator 430 (F430);Química Nova;2006-10
4. Redox Chemistry of Nickel Complexes in Aqueous Solutions;Chemical Reviews;2005-04-09
5. Nickel(II) and manganese(III) tetraazaannulenes complexes encapsulated in porous Vycor glass (PVG): investigation of catalytic activity;Journal of Molecular Catalysis A: Chemical;2004-11
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