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Title: Inactivation of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and spinach with the new affinity label 2-bromo-1,5-dihydroxy-3-pentanone 1,5-bisphosphate

Abstract

In an attempt to identify the active-site base believed to initiate catalysis by ribulosebisphosphate carboxylase, we have synthesized 2-bromo-1, 5-dihydroxy-3-pentanone 1,5-bisphosphate, a reactive analogue of a postulated intermediate of carboxylation. Although highly unstable, this compound can be shown to inactivate the carboxylases from both Rhodospirillum rubrum and spinach rapidly and irreversibly. Inactivation follows pseudo first-order kinetics, shows rate saturation and is greatly reduced by saturating amounts of the competitive inhibitor, 2-carboxyribitol 1,5-bisphosphate. The incorporation of reagent, quantified by reducing the modified carboxylases with (/sup 3/H)NaBH/sub 4/, shows that inactivation results from the modification of approximately one residue per catalytic subunit of the Rhodospirillum rubrum enzyme and less than one residue per protomeric unit of the spinach enzyme.

Authors:
 [1];
  1. Univ. of Tennessee, Oak Ridge
Publication Date:
OSTI Identifier:
5177575
DOE Contract Number:  
W-7405-ENG-26
Resource Type:
Journal Article
Journal Name:
Biochem. Biophys. Res. Commun.; (United States)
Additional Journal Information:
Journal Volume: 103:1
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BROMINATED ALIPHATIC HYDROCARBONS; CHEMICAL REACTIONS; CARBOXYLASE; INACTIVATION; CATALYSIS; BIOCHEMICAL REACTION KINETICS; OXYGENASES; LABELLED COMPOUNDS; PHOSPHATES; RHODOSPIRILLUM; SPINACH; TRITIUM COMPOUNDS; BACTERIA; ENZYMES; FOOD; HALOGENATED ALIPHATIC HYDROCARBONS; KINETICS; LIGASES; MICROORGANISMS; ORGANIC BROMINE COMPOUNDS; ORGANIC COMPOUNDS; ORGANIC HALOGEN COMPOUNDS; OXIDOREDUCTASES; OXYGEN COMPOUNDS; PHOSPHORUS COMPOUNDS; REACTION KINETICS; VEGETABLES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Donnelly, M I, and Hartman, F C. Inactivation of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and spinach with the new affinity label 2-bromo-1,5-dihydroxy-3-pentanone 1,5-bisphosphate. United States: N. p., 1981. Web. doi:10.1016/0006-291X(81)91674-0.
Donnelly, M I, & Hartman, F C. Inactivation of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and spinach with the new affinity label 2-bromo-1,5-dihydroxy-3-pentanone 1,5-bisphosphate. United States. https://doi.org/10.1016/0006-291X(81)91674-0
Donnelly, M I, and Hartman, F C. 1981. "Inactivation of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and spinach with the new affinity label 2-bromo-1,5-dihydroxy-3-pentanone 1,5-bisphosphate". United States. https://doi.org/10.1016/0006-291X(81)91674-0.
@article{osti_5177575,
title = {Inactivation of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and spinach with the new affinity label 2-bromo-1,5-dihydroxy-3-pentanone 1,5-bisphosphate},
author = {Donnelly, M I and Hartman, F C},
abstractNote = {In an attempt to identify the active-site base believed to initiate catalysis by ribulosebisphosphate carboxylase, we have synthesized 2-bromo-1, 5-dihydroxy-3-pentanone 1,5-bisphosphate, a reactive analogue of a postulated intermediate of carboxylation. Although highly unstable, this compound can be shown to inactivate the carboxylases from both Rhodospirillum rubrum and spinach rapidly and irreversibly. Inactivation follows pseudo first-order kinetics, shows rate saturation and is greatly reduced by saturating amounts of the competitive inhibitor, 2-carboxyribitol 1,5-bisphosphate. The incorporation of reagent, quantified by reducing the modified carboxylases with (/sup 3/H)NaBH/sub 4/, shows that inactivation results from the modification of approximately one residue per catalytic subunit of the Rhodospirillum rubrum enzyme and less than one residue per protomeric unit of the spinach enzyme.},
doi = {10.1016/0006-291X(81)91674-0},
url = {https://www.osti.gov/biblio/5177575}, journal = {Biochem. Biophys. Res. Commun.; (United States)},
number = ,
volume = 103:1,
place = {United States},
year = {Mon Nov 16 00:00:00 EST 1981},
month = {Mon Nov 16 00:00:00 EST 1981}
}