Application of pulse radiolysis to the study of proteins: chymotrypsin and trypsin
Journal Article
·
· Biophys. J.; (United States)
The one-electron reduction of chymotrypsin, trypsin, and their zymogens have been studied by pulse radiolysis. The optical spectra of the transient products from the two active enzymes display a pH-dependent band at 360 nm, associated with the histidine-electron adduct. The yield of the histidyl radical as a function of pH is consistent with a pK/suba/ < 4.5, which suggests that the radical is located at the enzyme active site. The histidines of the proenzymes chymotrypsinogen and trypsinogen are unreactive towards the hydrated electon. We conclude that formation of the histidine-electron adduct at the serine protease active site is sensitive to the physical alterations which accompany protease activation.
- Research Organization:
- Ohio State Univ., Columbus
- OSTI ID:
- 5761493
- Journal Information:
- Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 24:1; ISSN BIOJA
- Country of Publication:
- United States
- Language:
- English
Similar Records
$gamma$-radiolysis of trypsin, chymotrypsin, and chymotrypsinogen when associated with DNA
Reduction of Cu(II) complexes of histidine and histidyl peptides. A pulse radiolysis study. [Electrons]
Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state
Journal Article
·
Fri Mar 01 00:00:00 EDT 1974
· Radiat. Res., v. 57, no. 3, pp. 395-402
·
OSTI ID:4347406
Reduction of Cu(II) complexes of histidine and histidyl peptides. A pulse radiolysis study. [Electrons]
Journal Article
·
Sat Oct 01 00:00:00 EDT 1977
· Radiat. Res.; (United States)
·
OSTI ID:5335575
Conformational flexibility in the catalytic triad revealed by the high-resolution crystal structure of Streptomyces erythraeus trypsin in an unliganded state
Journal Article
·
Fri Feb 28 23:00:00 EST 2014
· Acta Crystallographica. Section D: Biological Crystallography
·
OSTI ID:22351313
Related Subjects
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ABSORPTION SPECTROSCOPY
ADDUCTS
AMINO ACIDS
AZOLES
CARBOXYLIC ACIDS
CHEMICAL RADIATION EFFECTS
CHEMICAL REACTIONS
CHEMISTRY
CHYMOTRYPSIN
DECOMPOSITION
ELECTRONS
ELEMENTARY PARTICLES
ENZYMES
FERMIONS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HISTIDINE
HYDRATION
HYDROLASES
HYDROXY ACIDS
IMIDAZOLES
LEPTONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEPTIDE HYDROLASES
PH VALUE
PROTEOLYSIS
RADIATION CHEMISTRY
RADIATION EFFECTS
RADIOLYSIS
REDUCTION
SERINE
SOLVATED ELECTRONS
SOLVATION
SPECTROSCOPY
TRYPSIN
59 BASIC BIOLOGICAL SCIENCES
ABSORPTION SPECTROSCOPY
ADDUCTS
AMINO ACIDS
AZOLES
CARBOXYLIC ACIDS
CHEMICAL RADIATION EFFECTS
CHEMICAL REACTIONS
CHEMISTRY
CHYMOTRYPSIN
DECOMPOSITION
ELECTRONS
ELEMENTARY PARTICLES
ENZYMES
FERMIONS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HISTIDINE
HYDRATION
HYDROLASES
HYDROXY ACIDS
IMIDAZOLES
LEPTONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PEPTIDE HYDROLASES
PH VALUE
PROTEOLYSIS
RADIATION CHEMISTRY
RADIATION EFFECTS
RADIOLYSIS
REDUCTION
SERINE
SOLVATED ELECTRONS
SOLVATION
SPECTROSCOPY
TRYPSIN