title: Chemical Posttranslational Modification with Designed Rhodium(II) Catalysts.
abstract: Natural enzymes use molecular recognition to perform exquisitely selective transformations on nucleic acids, proteins, and natural products. Rhodium(II) catalysts mimic this selectivity, using molecular recognition to allow selective modification of proteins with a variety of functionalized diazo reagents. The rhodium catalysts and the diazo reactivity have been successfully applied to a variety of protein folds, the chemistry succeeds in complex environments such as cell lysate, and a simple protein blot method accurately assesses modification efficiency. The studies with rhodium catalysts provide a new tool to study and probe protein-binding events, as well as a new synthetic approach to protein conjugates for medical, biochemical, or materials applications.
authors: Rice University, Houston, TX, United States.
authors: S C
authors: SC
authors: Martin
authors: Rice University, Houston, TX, United States.
authors: M B
authors: MB
authors: Minus
authors: Rice University, Houston, TX, United States. Electronic address: zb1@rice.edu.
authors: Z T
authors: ZT
authors: Ball
mesh_terms: D002384:Catalysis; D004798:Enzymes / Q000737:chemistry*; D015202:Protein Engineering; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry*; D012238:Rhodium / Q000737:chemistry*; D013237:Stereoisomerism; D018909:src Homology Domains
chemical_list: D004798:Enzymes; D011506:Proteins; D012238:Rhodium
keywords: Bioconjugation; Diazo; Enzyme design; Protein modification; Rhodium; SH3 domain