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The structure of Mn(II)-bound Rubisco from Spinacia oleracea.
Voland, Robert W; Coleman, Rachael E; Lancaster, Kyle M.
Afiliação
  • Voland RW; Department of Chemistry and Chemical Biology Cornell University, Baker Laboratory, 162 Sciences Drive, Ithaca, NY 14853, USA.
  • Coleman RE; Department of Chemistry and Chemical Biology Cornell University, Baker Laboratory, 162 Sciences Drive, Ithaca, NY 14853, USA.
  • Lancaster KM; Department of Chemistry and Chemical Biology Cornell University, Baker Laboratory, 162 Sciences Drive, Ithaca, NY 14853, USA. Electronic address: kml236@cornell.edu.
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.
Assuntos

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

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