about
Riboswitch effectors as protein enzyme cofactorsThe Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue that Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis † , ‡Cross-Link Formation of the Cysteine 228−Tyrosine 272 Catalytic Cofactor of Galactose Oxidase Does Not Require Dioxygen † ‡Isolation, cloning, mapping, and nucleotide sequencing of the gene encoding flavodoxin in Escherichia coli.Substituent effects on the ionization reaction of beta-mesylate phenethyl radicals.The anaerobic ribonucleoside triphosphate reductase from Escherichia coli requires S-adenosylmethionine as a cofactor.Ligand interactions with galactose oxidase: mechanistic insights.A conformational sampling model for radical catalysis in pyridoxal phosphate- and cobalamin-dependent enzymes.Enzymatic radical catalysis: coenzyme B12-dependent diol dehydratase.A proposal for reconsideration of the role of oxygen free radicals in cell differentiation and aging.Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase.Magnetic resonance of membranes.Isolation and initial characterization of a series of Chlamydia trachomatis isolates selected for hydroxyurea resistance by a stepwise procedureTwo conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.An autophosphorylating but not transphosphorylating activity is associated with the unique N terminus of the herpes simplex virus type 1 ribonucleotide reductase large subunit.The role of redox-active amino acids in the photosynthetic water-oxidizing complex.Model for magnetic field effects on radical pair recombination in enzyme kineticsAdenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Active holoenzyme produced from Escherichia coli.Radical-induced chain oxidation of proteins and its inhibition by chain-breaking antioxidantsDirect ESR detection or peroxynitrite-induced tyrosine-centred protein radicals in human blood plasma.Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme.Nitric oxide rapidly scavenges tyrosine and tryptophan radicals.Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro.Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase. Examination of the role of this residue in coenzyme-binding and catalysis.A conserved tyrosine in ferritin is a molecular capacitor.Synthesis and structural characterization of iron complexes bearing N-aryl-phenanthren-o-iminoquinone ligands.The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals.Amine Oxidases and Galactose OxidaseLearning from B enzymes: biomimetic and bioinspired catalysts for eco-friendly organic synthesis
P2860
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P2860
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Protein radical involvement in biological catalysis?
@en
type
label
Protein radical involvement in biological catalysis?
@en
prefLabel
Protein radical involvement in biological catalysis?
@en
P1476
Protein radical involvement in biological catalysis?
@en
P2093
P304
P356
10.1146/ANNUREV.BI.58.070189.001353
P577
1989-01-01T00:00:00Z