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Volume 137, Issue 7

Kinetic properties of ribulose bisphosphate carboxylase/oxygenase from , the putative symbiont of (Montagu), a bivalve mussel Free

Abstract

Some kinetic properties of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase from , a marine, facultatively heterotrophic, sulphur-oxidizing bacterium and putative symbiont of (Montagu), a bivalve mussel, have been determined. The kinetic parameters for the CO/Mg-activated enzyme were: (RuBP) 24·3 μ, (CO) 125·5 μ, K(O) 900 μ and (Mg) 1·53 m. The low CO affinity suggests that T. thyasiris may possess a CO-concentrating mechanism. RuBP oxygenase activity was inhibited by increasing CO concentration. Divalent metal ions were essential for RuBP carboxylase activity; activity of the Mg-free enzyme could be restored by the addition of Mg, Mn or Ca. The pH optimum was 7·8. The temperature optimum for RuBP carboxylase activity was 55 °C, although the enzyme rapidly lost activity at this temperature. An Arrhenius plot was biphasic, with a break at 40 °C. The activation energies were 55·5 × 10 J mol and 32·9 × 10 J mol over the temperature ranges 10–40 °C and 40–55 °C, respectively. was 2·12 for any 10 °C increment between 10·40 °C, and 1·47 between 40·55 °C. RuBP carboxylase activity was stable at 35 °C, the optimum growth temperature of . and at 7·5 °C, the temperature of the habitat of Thyasira flexuosa, but the activity was 40% and 3·5%, respectively, of the potential activity at 55 °C. RuBP carboxylase activity was stimulated by NaCl concentrations of up to 0·3 , with a maximum (33 %), occurring between 0·1 and 0·2 -NaCl. At higher concentrations of NaG (>0·3 ) RuBP carboxylase activity was inhibited

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1991-07-01
2024-04-30
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Kinetic properties of ribulose bisphosphate carboxylase/oxygenase from Thiobacillus thyasiris, the putative symbiont of Thyasira flexuosa (Montagu), a bivalve mussel
Microbiology 137, 1491 (1991); https://doi.org/10.1099/00221287-137-7-1491
/content/journal/micro/10.1099/00221287-137-7-1491
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