Molecular details of enzyme-substrate transients by resonance Raman spectroscopy
- 1 December 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Accounts of Chemical Research
- Vol. 16 (12) , 455-460
- https://doi.org/10.1021/ar00096a005
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Precise structural information for transient enzyme-substrate complexes by a combined x-ray crystallographic-resonance Raman spectroscopic approachBiochemistry, 1982
- Vibrational spectra of scissile bonds in enzyme active sites: a resonance Raman study of dithioacylpapainsBiochemistry, 1982
- Resonance-enhanced Raman identification of a ternary chemical intermediate during the equine liver alcohol dehydrogenase reduction of p-(dimethylamino)benzaldehydeBiochemistry, 1982
- Resonance Raman and electronic absorption spectral studies of some .beta.-(2-furyl)acryloylglyceraldehyde-3-phosphate dehydrogenasesBiochemistry, 1981
- Correlations between reactivity and structure of some chromophoric acylchymotrypsins by resonance Raman spectroscopyBiochemistry, 1981
- Evidence for two acyl group conformations in some furylacryloyl- and thienylacryloylchymotrypsins: resonance Raman studies of enzyme-substrate intermediates at pH 3.0Biochemistry, 1981
- 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
- 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