The Enzymatic Formation of Phosphoglyceric Acid From Ribulose Diphosphate and Carbon Dioxide

Weissbach, Arthur; Horecker, B.L.; Hurwitz, Jerard

doi:10.1016/s0021-9258(18)65843-0

Cited by 300 publications

(36 citation statements)

References 28 publications

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“…of the form II enzyme. The form I enzyme metal requirements correlate well with the requirements of the structurally similar plant carboxylase (16,24), whereas the form II enzyme metal requirements are analogous to the properties of the dimeric enzyme from R. rubrum (18). The rather restricted requirement for only Mg2" and Mn2" exhibited by the fonn II R. sphaeroides and R. rubrum enzymes may thus reflect a difference in the topography of the metal binding site(s) of carboxylases lacking small subunits.…”

Section: Resultsmentioning

confidence: 86%

Activation of ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides: probable role of the small subunit

Gibson¹,

Tabita²

1979

J Bacteriol

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The activation properties of the form I and form II ribulose 1,5-bisphosphate carboxylases from Rhodopseudomonas sphaeroides were examined. Both enzymes have a requirement of Mg2+ for optimal activity. Mn2+, Ni2+, and Co2+ can also support activity of the form I enzyme, whereas only Mn2+ can substitute for Mg2+ with the form II enzyme. The effect of different preincubations on the carboxylase reaction was also examined. Both enzymes exhibited a lag when preincubated with other than Mg2+ and CO2 before assay, but the lag was much more pronounced and the rate of the reaction was slower with the form I enzyme under these conditions. Activation of the form I carboxylase By Mg2+ and CO2 occurred more rapidly than that of the form II enzyme. The results obtained with the two distinct forms of carboxylase from R. sphaeroides, as well as studies with the spinach and Rhodospirillum rubrum enzymes, thus indicate that the presence of the small subunit affects the rate of activation by Mg2+ and CO2 as well as the rate of reactivation of ribulose bisphosphate-inactivated enzyme.

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Section: Resultsmentioning

confidence: 86%

Activation of ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides: probable role of the small subunit

Gibson¹,

Tabita²

1979

J Bacteriol

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“…In fact, solution studies revealed that the glycerate-3-P formed by nonenzymatic hydrolysis of 3 was a mixture of D-and lglycerate-3-P and that the L-glycerate-3-F was derived from C-l, C-2, and C-2' of 3 (Siegel & Lane, 1973). In contrast, two molecules of o-glycerate-3-P are produced in the enzymatic reaction (Weissbach et al, 1956;Jakoby et al, 1956). This difference in the enzymatic and nonenzymatic reactions might be explained by postulating a glycerate-3-P epimerase activity in ribulose-P2 carboxylase/oxygenase, a carbanion inversion mechanism, or other, less likely mechanisms involving an electron-deficient carbon at C-2 of 3.…”

Section: Interaction Of the Carboxypentitol Bisphosphates Withmentioning

confidence: 99%

“…The initial step is the enolization of ribulose-P2 (1) to form 2, which is attacked by C02 to form a 2-C-carboxy-3-ketopentitol bisphosphate, 3. Addition of H20 across the bond at C-2 and C-3 of 3 yields two molecules of o-glycerate-3-P (Fiedler et al, 1967 , 1969; Miillhofer & Rose, 1965; Pierce et al, 1980;Weissbach et al, 1956;Jakoby et al, 1956). In addition, the oxygen atoms at C-2 and C-3 of ribulose-P2 are retained in the products of the carboxylation reaction, ruling" out the intermediacy of eneamine or dithioacetal derivatives in the reaction (Sue & Knowles, 1978;Lorimer, 1978).…”

mentioning

confidence: 99%

Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogs

Pierce¹,

Tolbert²,

Barker³

1980

Biochemistry

284

225

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2-C-Carboxy-D-ribitol 1,5-bisphosphate and 2-C-carboxy-D-arabinitol 1,5-bisphosphate have been synthesized, purified, and characterized. In the presence of Mg2+, 2-C-carboxy-D-arabinitol 1,5-bisphosphate binds to ribulose-1,5-bisphosphate carboxylase/oxygenase by a two-step mechanism. The first, rapid step is similar to the binding of ribulose 1,5-bisphosphate or its structural analogues. The second step is a slower process (k = 0.04 s-1) and accounts for the tighter binding of 2-C-carboxy-D-arabinitol 1,5-bisphosphate (Kd less than or approximately to 10(-11) M) than of 2-C-carboxy-D-ribitol 1,5-bisphosphate (Kd = 1.5 X 10(6) M). Both carboxypentitol bisphosphates exhibit competitive inhibition with respect to ribulose 1,5-bisphosphate. 2-C-(Hydroxymethyl)-D-ribitol 1,5-bisphosphate and 2-C-(hydroxymethyl)-D-arabinitol 1,5-bisphosphate were also synthesized; both are competitive inhibitors with respect to ribulose 1,5-bisphosphate with Ki = 8.0 X 10(-5) M and Ki = 5.0 X 10(-6) M, respectively. Thus, the carboxyl group of 2-C-carboxy-D-arabinitol 1,5-bisphosphate is necessary for maximal interaction with the enzyme. Additionally, Mg2+ is essential for the tight binding of 2-C-carboxy-D-arabinitol 1,5-bisophsphate. A model for catalysis of ribulose 1,5-bisphosphate carboxylation is discussed which includes a functional role for Mg2+ in the stabilization of the intermediate 2-C-carboxy-3-keto-D-arabinitol 1,5-bisphosphate. Mechanistic implications that arise from the stereochemistry of this intermediate are also discussed.

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“…Nearly all carbon in the biosphere enters by CO 2 fixation in the Calvin-Benson-Bassham cycle (Bassham, 2003;Bassham et al, 1954;Benson, 2002;Field et al, 1998;Raven, 2009). Ribulose Bisphosphate Carboxylase/Oxygenase -commonly known as rubisco -is the CO 2 fixing enzyme in this cycle (Kawashima and Wildman, 1971;Weissbach et al, 1956;Wildman, 2002) and likely the most abundant enzyme on Earth (Bar-On and Milo, 2019). As rubisco is abundant and central to biology, one might expect it to be an exceptional catalyst, but it is not.…”

Section: Introductionmentioning

confidence: 99%

Functional reconstitution of a bacterial CO2 concentrating mechanism in Escherichia coli

Flamholz

Dugan

Blikstad

et al. 2020

eLife

102

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Many photosynthetic organisms employ a CO2 concentrating mechanism (CCM) to increase the rate of CO2 fixation via the Calvin cycle. CCMs catalyze ≈50% of global photosynthesis, yet it remains unclear which genes and proteins are required to produce this complex adaptation. We describe the construction of a functional CCM in a non-native host, achieved by expressing genes from an autotrophic bacterium in an E. coli strain engineered to depend on rubisco carboxylation for growth. Expression of 20 CCM genes enabled E. coli to grow by fixing CO2 from ambient air into biomass, with growth in ambient air depending on the components of the CCM. Bacterial CCMs are therefore genetically compact and readily transplanted, rationalizing their presence in diverse bacteria. Reconstitution enabled genetic experiments refining our understanding of the CCM, thereby laying the groundwork for deeper study and engineering of the cell biology supporting CO2 assimilation in diverse organisms.

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The Enzymatic Formation of Phosphoglyceric Acid From Ribulose Diphosphate and Carbon Dioxide

Cited by 300 publications

References 28 publications

Activation of ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides: probable role of the small subunit

Activation of ribulose 1,5-bisphosphate carboxylase from Rhodopseudomonas sphaeroides: probable role of the small subunit

Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogs

Functional reconstitution of a bacterial CO2 concentrating mechanism in Escherichia coli

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