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Title: /sup 13/C nuclear magnetic resonance study of the CO/sub 2/ activation of ribulosebisphosphate carboxylase from Rhodospirillum rubrum

Abstract

Ribulosebisphosphate carboxylase (3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) from Rhodospirillum rubrum is activated by CO/sub 2/ and Mg/sup 2 +/. /sup 13/C NMR spectra were determined for the unactivated enzyme and for enzyme that had been activated by /sup 13/CO/sub 2/ and Mg/sup 2 +/. In addition to the expected resonance for H/sup 13/CO/sub 3//sup -//CO/sub 3//sup 2 -/ at 161.8 ppM downfield from tetramethylsilane, the spectrum of the activated enzyme shows a broad resonance at 164.9 ppM. Analogy with previous NMR studies of /sup 13/CO/sub 2/ binding to hemoglobin suggests that the CO/sub 2/ activation of ribulosebisphosphate carboxylase involves formation of a carbamate between an enzyme amino group and CO/sub 2/.

Authors:
 [1]; ;
  1. (Univ. of Wisconsin, Madison)
Publication Date:
OSTI Identifier:
5099414
DOE Contract Number:  
W-7405-ENG-26
Resource Type:
Journal Article
Journal Name:
Proc. Natl. Acad. Sci. U.S.A.; (United States)
Additional Journal Information:
Journal Volume: 76:2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CARBON 13; TRACER TECHNIQUES; CARBON DIOXIDE; BIOCHEMICAL REACTION KINETICS; CARBOXYLASE; CARBAMATES; ENZYME ACTIVITY; INTERMEDIATE STRUCTURE; LABELLED COMPOUNDS; MAGNESIUM IONS; NUCLEAR MAGNETIC RESONANCE; PHOTOSYNTHESIS; PLANTS; CARBON COMPOUNDS; CARBON ISOTOPES; CARBON OXIDES; CARBONIC ACID DERIVATIVES; CARBOXYLIC ACID SALTS; CHALCOGENIDES; CHARGED PARTICLES; CHEMICAL REACTIONS; ENZYMES; EVEN-ODD NUCLEI; IONS; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; LIGHT NUCLEI; LYASES; MAGNETIC RESONANCE; NUCLEI; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; OXIDES; OXYGEN COMPOUNDS; PHOTOCHEMICAL REACTIONS; REACTION KINETICS; RESONANCE; STABLE ISOTOPES; SYNTHESIS; 550201* - Biochemistry- Tracer Techniques; 551001 - Physiological Systems- Tracer Techniques

Citation Formats

O'Leary, M.H., Joworski, R.J., and Hartman, F.C. /sup 13/C nuclear magnetic resonance study of the CO/sub 2/ activation of ribulosebisphosphate carboxylase from Rhodospirillum rubrum. United States: N. p., 1979. Web. doi:10.1073/pnas.76.2.673.
O'Leary, M.H., Joworski, R.J., & Hartman, F.C. /sup 13/C nuclear magnetic resonance study of the CO/sub 2/ activation of ribulosebisphosphate carboxylase from Rhodospirillum rubrum. United States. doi:10.1073/pnas.76.2.673.
O'Leary, M.H., Joworski, R.J., and Hartman, F.C. Thu . "/sup 13/C nuclear magnetic resonance study of the CO/sub 2/ activation of ribulosebisphosphate carboxylase from Rhodospirillum rubrum". United States. doi:10.1073/pnas.76.2.673.
@article{osti_5099414,
title = {/sup 13/C nuclear magnetic resonance study of the CO/sub 2/ activation of ribulosebisphosphate carboxylase from Rhodospirillum rubrum},
author = {O'Leary, M.H. and Joworski, R.J. and Hartman, F.C.},
abstractNote = {Ribulosebisphosphate carboxylase (3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) from Rhodospirillum rubrum is activated by CO/sub 2/ and Mg/sup 2 +/. /sup 13/C NMR spectra were determined for the unactivated enzyme and for enzyme that had been activated by /sup 13/CO/sub 2/ and Mg/sup 2 +/. In addition to the expected resonance for H/sup 13/CO/sub 3//sup -//CO/sub 3//sup 2 -/ at 161.8 ppM downfield from tetramethylsilane, the spectrum of the activated enzyme shows a broad resonance at 164.9 ppM. Analogy with previous NMR studies of /sup 13/CO/sub 2/ binding to hemoglobin suggests that the CO/sub 2/ activation of ribulosebisphosphate carboxylase involves formation of a carbamate between an enzyme amino group and CO/sub 2/.},
doi = {10.1073/pnas.76.2.673},
journal = {Proc. Natl. Acad. Sci. U.S.A.; (United States)},
number = ,
volume = 76:2,
place = {United States},
year = {1979},
month = {2}
}