Reversible inhibition of  CO 2   fixation by ribulose 1,5‐bisphosphate carboxylase/oxygenase through the synergic effect of arsenite and a monothiol | Zendy

SUDHANI HEMANTH P. K. | Zendy; GARCíAMURRIA MARíAJESúS | Zendy; MORENO JOAQUíN | Zendy

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Reversible inhibition of CO 2 fixation by ribulose 1,5‐bisphosphate carboxylase/oxygenase through the synergic effect of arsenite and a monothiol

Author(s) -

SUDHANI HEMANTH P. K.,

GARCíAMURRIA MARíAJESúS,

MORENO JOAQUíN

Publication year - 2013

Publication title -

plant, cell and environment

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.646

H-Index - 200

eISSN - 1365-3040

pISSN - 0140-7791

DOI - 10.1111/pce.12050

Subject(s) - arsenite , ribulose 1,5 bisphosphate , rubisco , pyruvate carboxylase , ribulose , oxygenase , chemistry , biochemistry , glutathione , carbon fixation , photosynthesis , enzyme , arsenic , organic chemistry

The photosynthetic carbon‐fixing enzyme, ribulose 1,5‐bisphosphate carboxylase/oxygenase ( R ubisco), is reversibly inhibited by micromolar arsenite in the presence of an enhancer monothiol such as cysteine, cysteamine, 2‐mercaptoethanol or N ‐acetylcysteine, but not glutathione. Arsenite reacts specifically with the vicinal C ys172‐ C ys192 from the large subunit of Rubisco and with the monothiol to establish a ternary complex. The combination of arsenite and monothiol stops also the carbon fixation in illuminated cultures of C hlamydomonas reinhardtii but the in vivo arrest appears to be driven by an undetermined effector that is even more sensitive to the arsenite‐thiol synergism than R ubisco.

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