Rapid-scanning cryospectroscopy of enzyme-substrate-inhibitor complexes of cobalt carboxypeptidase A
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00366a025
Reference19 articles.
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2. Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides
3. Carboxypeptidase A. Differences in the mechanisms of ester and peptide hydrolysis
4. Approach to inhibition kinetics. Measurement of enzyme-substrate complexes by electronic energy transfer
5. Cryospectrokinetic characterization of intermediates in biochemical reactions: carboxypeptidase A.
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1. Characterization of “spectroscopically quiet” metals in biology;Coordination Chemistry Reviews;2005-01
2. Zinc catalysis in metalloproteases;Metal Sites in Proteins and Models;1997
3. A time-resolved study of substrate hydrolysis of carboxypeptidase A;Physica B: Condensed Matter;1995-03
4. The enzymatic mechanism of carboxypeptidase: A molecular dynamics study;Proteins: Structure, Function, and Genetics;1994-02
5. [23] Low-temperature stopped-flow rapid-scanning spectroscopy: Performance tests and use of aqueous salt cryosolvents;Metallobiochemistry Part C: Spectroscopic and Physical Methods for Probing Metal Ion Environments in Metalloenzymes and Metalloproteins;1993
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