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

Journal Article · Mon Mar 21 00:00:00 EST 1977 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(77)91045-2· OSTI ID:7302951

Schloss, J V; Hartman, F C

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.

• Research Organization: Univ. of Tennessee, Oak Ridge
• OSTI ID: 7302951
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Vol. 75:2
• Country of Publication: United States
• Language: English

Related Subjects

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