Modification of Rhodospirillum rubrum ribulose bisphosphate carboxylase with pyridoxal phosphate. 2. Stoichiometry and kinetics of inactivation.

Abstract:

:Rhodospirillum rubrum ribulose bisphosphate carboxylase contains two high affinity binding sites for pyridoxal phosphate and two catalytic sites per dimer. However, pyridoxal phosphate binding at only one site is sufficient for inactivation of both catalytic sites. In the presence of 20 mM bicarbonate, 10 mM magnesium, and pyridoxal phosphate, the rates of inactivation and Schiff base formation are pseudo-first-order and show saturation kinetics. These observations provide additional evidence that pyridoxal phosphate binds at the active site of the R. rubrum carboxylase. It is also proposed that the large subunit may contain regulatory as well as catalytic properties.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Whitman WB,Tabita FR

doi

10.1021/bi00600a024

subject

Has Abstract

pub_date

1978-04-04 00:00:00

pages

1288-93

issue

7

eissn

0006-2960

issn

1520-4995

journal_volume

17

pub_type

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