Kinetics and mechanism studies in biomimetic chemistry: metalloenzyme model systems
نویسندگان
چکیده
منابع مشابه
Kinetics and mechanism studies in biomimetic chemistry: metalloenzyme model systems
To understand the biological transport and utilization of dioxygen at the level of mechanistic chemistry it has been necessary to synthesize small molecules (active site sections) which carry out the binding or catalytic function. We have prepared iron porphyrin compounds which mimic the dioxygen binding to myoglobin and the oxidations catalyzed by peroxidases and related enzymes. Using a combi...
متن کاملSwitch-functionalized systems in biomimetic chemistry
A variety of switch—functionalized crown ethers have been synthesized. They change their chemical and physical properties in response to the stimuli from the outside world such as light, redox, heat, etc. These novel crown ethers act as ion carriers in membrane transport systems. The rate of ion transport can be thus controlled by an on—off—type switch.
متن کاملBiomimetic chemistry
Several cases are described in which the chelate effect contributes to binding and catalysis. In the first examples, dimers made up of linked cyclodextrins show very strong selective substrate binding, and with catalytic groups in the linkers they are effective catalysts of reactions of bound substrates. In later examples, chelate binding of transition states by a base and an acid produce effec...
متن کاملAcid Catalysed Condesation of Phloroglucinol and Acetone-Kinetics and Mechanism
The kinetic study of the condensation reaction between phloroglucinol and acetone was investigated at 30, 35, 40 and 45±0.05 °C in 100% methanol. The hydrochloric acid concentrations used were 0.0261, 0.0364, 0.0577 and 0.0728 M. The reaction was investigated with and without a promoter, thioglycollic acid (TGA), and taking into account the functionality (h<e...
متن کاملDissecting the mechanism of oxygen trafficking in a metalloenzyme.
A key question in the biological activation of oxygen is how the protein matrix regulates the delivery of oxygen to its site of activation. We are using Escherichia coli copper amine oxidase as a model system to investigate the roles played by both local active site residues as well as long range interactions in this process. We have generated active site mutants, as well as mutants in the puta...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Pure and Applied Chemistry
سال: 1991
ISSN: 1365-3075,0033-4545
DOI: 10.1351/pac199163020265