Characterization of the Zinc Binding Site in Methionine Synthase Enzymes of Escherichia coli: The Role of Zinc in the Methylation of Homocysteine
- 1 August 1998
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (33), 8410-8416
- https://doi.org/10.1021/ja980581g
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- The Limitations of X-ray Absorption Spectroscopy for Determining the Structure of Zinc Sites in Proteins. When Is a Tetrathiolate Not a Tetrathiolate?Journal of the American Chemical Society, 1998
- Methylcobamide:Coenzyme M Methyltransferase Isozymes from Methanosarcina barkeriJournal of Biological Chemistry, 1996
- A Synthetic Module for the metH Gene Permits Facile Mutagenesis of the Cobalamin-Binding Region of Escherichia coli Methionine Synthase: Initial Characterization of Seven Mutant ProteinsBiochemistry, 1996
- Cobalamin-Independent Methionine Synthase from Escherichia coli: A Zinc MetalloenzymeBiochemistry, 1996
- Vitamin-B12-Independent Methionine Synthase from a Higher Plant (Catharanthus Roseus). Molecular Characterization, Regulation, Heterologous Expression, and Enzyme PropertiesEuropean Journal of Biochemistry, 1995
- How a Protein Binds B 12 : A 3.0 Å X-Ray Structure of B 12 -Binding Domains of Methionine SynthaseScience, 1994
- Methylation Dependent Functional Switch Mechanism Newly Found in the Escherichia coli Ada ProteinJournal of the American Chemical Society, 1994
- Zinc: biological functions and coordination motifsAccounts of Chemical Research, 1993
- Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problemBiochemistry, 1992
- Trigonal planar [Zn(SR)3]1- complex. A possible new coordination mode for zinc-cysteine centersJournal of the American Chemical Society, 1989