The structure and dynamics of enzyme-substrate reaction intermediates determined by resonance Raman spectroscopy
- 1 January 1985
- journal article
- research article
- Published by Walter de Gruyter GmbH in Pure and Applied Chemistry
- Vol. 57 (2) , 225-234
- https://doi.org/10.1351/pac198557020225
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- Comparison of the substrate conformations in the active sites of papain, chymopapain, ficin and bromelain by resonance Raman spectroscopyBiochemical and Biophysical Research Communications, 1983
- Precise structural information for transient enzyme-substrate complexes by a combined x-ray crystallographic-resonance Raman spectroscopic approachBiochemistry, 1982
- Evidence for two acyl group conformations in some furylacryloyl- and thienylacryloylchymotrypsins: resonance Raman studies of enzyme-substrate intermediates at pH 3.0Biochemistry, 1981
- The Internal Dynamics of Globular ProteinCritical Reviews in Biochemistry, 1981
- Structure of actinidin, after refinement at 1.7 Å resolutionJournal of Molecular Biology, 1980
- The use of resonance Raman spectroscopy to monitor catalytically important bonds during enzymic catalysis. Application to the hydrolysis of methyl thionohippurate by papain.Journal of Biological Chemistry, 1979
- Resonance Raman investigation of β-(2-furyl)-acryloyl-glyceraldehyde-3-phosphate dehydrogenaseFEBS Letters, 1978
- Charge effects in the active site of papain: resonance Raman and absorption evidence for electron polarization occurring in the acyl group of some acylpapainsBiochemistry, 1978
- Resonance Raman evidence for substrate reorganization in the active site of papainBiochemistry, 1976
- DIRECT EVIDENCE FOR AN ACYLATED THIOL AS AN INTERMEDIATE IN PAPAIN- AND FICIN-CATALYSED HYDROLYSESBiochemical Journal, 1965