Cofactor-dependent Assembly of the Flavoenzyme Vanillyl-alcohol Oxidase
Open Access
- 1 September 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (39) , 36425-36432
- https://doi.org/10.1074/jbc.m205841200
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Asp-170 Is Crucial for the Redox Properties of Vanillyl-alcohol OxidaseJournal of Biological Chemistry, 2000
- Electrospray Ionization Mass Spectrometric Determination of the Molecular Mass of the ∼200-kDa Globin Dodecamer Subassemblies in Hexagonal Bilayer HemoglobinsJournal of Biological Chemistry, 1999
- Selective association of protein molecules followed by mass spectrometryProtein Science, 1999
- Detection of a Monomeric Intermediate Associated with Dimerization of Protein Hu by Mass SpectrometryJournal of the American Chemical Society, 1998
- Probing the Nature of Noncovalent Interactions by Mass Spectrometry. A Study of Protein−CoA Ligand Binding and AssemblyJournal of the American Chemical Society, 1996
- The Cytochrome Subunit Is Necessary for Covalent FAD Attachment to the Flavoprotein Subunit of p-Cresol MethylhydroxylasePublished by Elsevier ,1995
- Trapping, detection and reaction of very large single molecular ions by mass spectrometryNature, 1994
- Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltonsAnalytical Chemistry, 1988
- Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprintJournal of Molecular Biology, 1986
- Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductaseJournal of Molecular Biology, 1983