New method for determining the intrinsic deactivation rate constant

AIChE Journal ◽  
1988 ◽  
Vol 34 (4) ◽  
pp. 692-693 ◽  
Author(s):  
Marek Wojcik
Keyword(s):  
Rate Constant ◽  
New Method ◽  
Deactivation Rate ◽  
Deactivation Rate Constant

Atomic Layer Deposition for Improved Stability of Catalysts for the Conversion of Biomass to Chemicals and Fuels

2011 ◽  
Vol 1366 ◽  
Author(s):  
Monika K. Wiedmann ◽  
Yomaira J. Pagan-Torres ◽  
Mark H. Tucker ◽  
James A. Dumesic ◽  
T. F. Kuech
Keyword(s):  
Atomic Layer Deposition ◽  
Metal Oxides ◽  
Rate Constant ◽  
Flow Reactor ◽  
Atomic Layer ◽  
Deactivation Rate ◽  
Layer Deposition ◽  
Improved Stability ◽  
Deactivation Rate Constant ◽  
Acid Catalyzed

ABSTRACTAtomic layer deposition (ALD) has been used to coat SBA-15 and functionalized SBA-15 with various metal oxides. Use of SBA-15 coated with 4-10 ALD cycles of titania, alumina, niobia, or zirconia in the acid-catalyzed dehydration of fructose to 5-hydroxymethylfurfural (HMF) resulted in 24-57% conversion, with 0-22% selectivity, at 130 °C with 2 wt % fructose in 4:1 THF:H2O. Propylsulfonic acid functionalized SBA-15 (SBA-15-PrSO3H) had a 25% conversion and 48% selectivity for HMF under the same conditions. SBA-15-PrSO3H was also coated with 2 ALD cycles of titania followed by 8 ALD cycles silica. The deactivation rate constant for SBA-15-PrSO3H was 2.7 x 10-2 h-1 for the dehydration of fructose to HMF in a flow reactor at 130 °C with a feed of 2 wt % fructose in 4:1 THF:H2O. In comparison, the deactivation rate constant for the ALD coated SBA-15-PrSO3H-ALD was 7.9 x 10-3 h-1.

scholarly journals The role of the C-terminal tail of flavocytochrome b2

1989 ◽  
Vol 263 (3) ◽  
pp. 849-853 ◽  
Author(s):  
S A White ◽  
M T Black ◽  
G A Reid ◽  
S K Chapman
Keyword(s):  
Rate Constant ◽  
Structural Integrity ◽  
Lactate Concentration ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Original Activity ◽  
First Order ◽  
Flavocytochrome B2 ◽  
Deactivation Rate ◽  
Deactivation Rate Constant

A flavocytochrome b2 (L-lactate dehydrogenase) mutant was constructed in which the C-terminal tail (23 amino acid residues) had been deleted (Gly-489→Stop). This tail appears to form many intersubunit contacts in the tetrameric wild-type protein, and it was expected that its removal might lead to the formation of monomeric flavocytochrome b2. The isolated tail-deleted mutant enzyme (TD-b2), however, was found to be tetrameric (Mr 220,000). TD-b2 shows Km and kcat. values (at 25 degrees C and pH 7.5) of 0.96 +/- 0.06 mM and 165 +/- 6 s-1 respectively compared with 0.49 +/- 0.04 mM and 200 +/- 10 s-1 for the wild-type enzyme. The kinetic isotope effect with [2-2H]lactate as substrate seen for TD-b2, with ferricyanide as electron acceptor, was essentially the same as that observed for the wild-type enzyme. TD-b2 exhibited loss of activity during turnover in a biphasic process. The rate of the faster of the two phases was dependent on L-lactate concentration and at saturating concentrations showed a first-order deactivation rate constant, kf(deact.), of 0.029 s-1 (at 25 degrees C and pH 7.5). The slower phase, however, was independent of L-lactate concentration and gave a first-order deactivation rate constant, ks(deact.), of 0.01 s-1 (at 25 degrees C and pH 7.5). This slower phase was found to correlate with dissociation of FMN, which is one of the prosthetic groups of the enzyme. Thus fully deactivated TD-b2, which was also tetrameric, was found to be completely devoid of FMN. Much of the original activity of TD-b2 could be recovered by re-incorporation of FMN. Thus the C-terminal tail of flavocytochrome b2 appears to be required for the structural integrity of the enzyme around the flavin active site even though the two are well separated in space.

Predictive modeling of the total deactivation rate constant of singlet oxygen by heterocyclic compounds

2009 ◽  
Vol 28 (1) ◽  
pp. 12-19 ◽  
Author(s):  
Andrew G. Mercader ◽  
Pablo R. Duchowicz ◽  
Francisco M. Fernández ◽  
Eduardo A. Castro ◽  
Franco M. Cabrerizo ◽  
...  
Keyword(s):  
Singlet Oxygen ◽  
Rate Constant ◽  
Predictive Modeling ◽  
Heterocyclic Compounds ◽  
Deactivation Rate ◽  
Deactivation Rate Constant

Collisional Deactivation Rates of Electronically Excited Molecular Ions. II

1972 ◽  
Vol 50 (1) ◽  
pp. 1-7 ◽  
Author(s):  
G. I. Mackay ◽  
R. E. March
Keyword(s):  
Rate Constants ◽  
Radiative Lifetime ◽  
Molecular Ions ◽  
Deactivation Rate ◽  
Complete Knowledge ◽  
Induced Dipole ◽  
Excited Species ◽  
Vibrational Levels ◽  
Electronically Excited ◽  
Deactivation Rate Constant

Total deactivation rate constants have been determined for N2+(B2Σu+) and the (A2Πu) and (B2Σu+) states of CO2+ with a number of quenchers. The energy specific total deactivation rate constant is compared to the total radiative lifetime of the excited species. A particular novelty of the technique is that it does not require a complete knowledge of the formation modes for the excited species. The results are compared with theoretical values obtained from the ion-induced dipole model. Individual deactivation rate constants are presented for N2+(B2Σu+) ions in the v = 0, 1, and 2 vibrational levels quenched by N2, O2, H2, and CO2; and for the(A2Πu) and (B2Σu+) states of CO2+ quenched byCO2, N2, O2, NO, and H2. Charge transfer is the most probable mode of deactivation except in the CO2+–H2 reactions where H-atom abstraction is more probable.

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