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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

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
 [1];
  1. Univ. of Tennessee, Oak Ridge
+ Show Author Affiliations

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.

DOE Contract Number:
W-7405-ENG-26
OSTI ID:
5177575
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 103:1; ISSN BBRCA
Country of Publication:
United States
Language:
English

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Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
BIOCHEMICAL REACTION KINETICS
BROMINATED ALIPHATIC HYDROCARBONS
CARBOXYLASE
CATALYSIS
CHEMICAL REACTIONS
ENZYMES
FOOD
HALOGENATED ALIPHATIC HYDROCARBONS
INACTIVATION
KINETICS
LABELLED COMPOUNDS
LIGASES
MICROORGANISMS
ORGANIC BROMINE COMPOUNDS
ORGANIC COMPOUNDS
ORGANIC HALOGEN COMPOUNDS
OXIDOREDUCTASES
OXYGEN COMPOUNDS
OXYGENASES
PHOSPHATES
PHOSPHORUS COMPOUNDS
REACTION KINETICS
RHODOSPIRILLUM
SPINACH
TRITIUM COMPOUNDS
VEGETABLES