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Title: Reaction of ribulosebisphosphate carboxylase from Rhodospirillum rubrum with the potential affinity label 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate

Abstract

Under mild conditions, 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate rapidly and irreversibly inactivates ribulosebisphosphate carboxylase from Rhodospirillum rubrum. The substrate ribulosebisphosphate protects the enzyme against inactivation. Incorporation of reagent has been quantitated by reduction of the modified carboxylase with (/sup 3/H)NaBH/sub 4/. Based on the difference in the levels of incorporation found in the inactivated enzyme as compared with the protected enzyme, loss of enzymic activity results from the modification of about 0.4 residue per catalytic subunit. Analyses of hydrolysates demonstrate that both cysteinyl and lysyl derivatives are present in the inactivated carboxylase; the protected sample contains about the same amount of modified cysteine but little of the modified lysine. Thus, inactivation appears to correlate with derivatization of lysyl residues.

Authors:
;
Publication Date:
Research Org.:
Univ. of Tennessee, Oak Ridge
OSTI Identifier:
7302951
Resource Type:
Journal Article
Journal Name:
Biochem. Biophys. Res. Commun.; (United States)
Additional Journal Information:
Journal Volume: 75:2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CARBOXYLASE; CHEMICAL ACTIVATION; RHODOSPIRILLUM; BIOCHEMICAL REACTION KINETICS; CATALYSIS; CYSTEINE; ENZYMES; LYSINE; METABOLISM; AMINO ACIDS; BACTERIA; CARBOXYLIC ACIDS; KINETICS; LYASES; MICROORGANISMS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; REACTION KINETICS; THIOLS; 550200* - Biochemistry; 550700 - Microbiology

Citation Formats

Schloss, J V, and Hartman, F C. Reaction of ribulosebisphosphate carboxylase from Rhodospirillum rubrum with the potential affinity label 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate. United States: N. p., 1977. Web. doi:10.1016/0006-291X(77)91045-2.
Schloss, J V, & Hartman, F C. Reaction of ribulosebisphosphate carboxylase from Rhodospirillum rubrum with the potential affinity label 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate. United States. https://doi.org/10.1016/0006-291X(77)91045-2
Schloss, J V, and Hartman, F C. Mon . "Reaction of ribulosebisphosphate carboxylase from Rhodospirillum rubrum with the potential affinity label 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate". United States. https://doi.org/10.1016/0006-291X(77)91045-2.
@article{osti_7302951,
title = {Reaction of ribulosebisphosphate carboxylase from Rhodospirillum rubrum with the potential affinity label 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate},
author = {Schloss, J V and Hartman, F C},
abstractNote = {Under mild conditions, 3-bromo-1,4-dihydroxy-2-butanone 1,4-bisphosphate rapidly and irreversibly inactivates ribulosebisphosphate carboxylase from Rhodospirillum rubrum. The substrate ribulosebisphosphate protects the enzyme against inactivation. Incorporation of reagent has been quantitated by reduction of the modified carboxylase with (/sup 3/H)NaBH/sub 4/. Based on the difference in the levels of incorporation found in the inactivated enzyme as compared with the protected enzyme, loss of enzymic activity results from the modification of about 0.4 residue per catalytic subunit. Analyses of hydrolysates demonstrate that both cysteinyl and lysyl derivatives are present in the inactivated carboxylase; the protected sample contains about the same amount of modified cysteine but little of the modified lysine. Thus, inactivation appears to correlate with derivatization of lysyl residues.},
doi = {10.1016/0006-291X(77)91045-2},
url = {https://www.osti.gov/biblio/7302951}, journal = {Biochem. Biophys. Res. Commun.; (United States)},
number = ,
volume = 75:2,
place = {United States},
year = {1977},
month = {3}
}