The structure of Mn(II)-bound Rubisco from Spinacia oleracea.
J Inorg Biochem
; 260: 112682, 2024 Nov.
Article
em En
| MEDLINE
| ID: mdl-39094246
ABSTRACT
The rate of photosynthesis and, thus, CO2 fixation, is limited by the rate of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Not only does Rubisco have a relatively low catalytic rate, but it also is promiscuous regarding the metal identity in the active site of the large subunit. In Nature, Rubisco binds either Mg(II) or Mn(II), depending on the chloroplastic ratio of these metal ions; most studies performed with Rubisco have focused on Mg-bound Rubisco. Herein, we report the first crystal structure of a Mn-bound Rubisco, and we compare its structural properties to those of its Mg-bound analogues.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ribulose-Bifosfato Carboxilase
/
Spinacia oleracea
/
Manganês
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article