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At least 127 records · Page 7Linked to original sources

PubMed2003

Evaluation of oxygen uptake kinetics and oxygen kinetics of peripheral skeletal muscle during recovery from exercise in patients with chronic obstructive pulmonary disease.

The biochemical features of skeletal muscle and its contribution to exercise intolerance in patients with chronic obstructive pulmonary disease (COPD) is under active investigation. Near-infrared spectroscopy (NIRS) can non-invasively provide information on the oxidative capacity of muscle. To clarify whether oxygenation of peripheral muscle is one determinant of exercise tolerance, we simultaneously examined the oxygen uptake (V O 2off) kinetics and oxygen kinetics of peripheral skeletal muscle evaluated by NIRS during recovery from exercise in COPD patients. Fifteen patients with COPD and five normal control subjects performed a symptom-limited incremental exercise test. On the following day, all patients performed a constant work rate exercise test while being monitored using NIRS continuously for changes in concentration of oxygenated haemoglobin (HbO2) and during expired gas analysis. We found that the time constant of during recovery from constant work rate exercise (V O 2off) and the time constant of V O 2off during recovery (tau V O 2off) were significantly longer in COPD patients than in normal control subjects. was inversely correlated with absolute values of forced expiratory volume in 1 s (FEV1.0) and FEV1.0 (% predicted). However, no significant correlation was found between and FVC (forced vital capacity), FEV1.0/FVC, or diffusing capacity of the lung for CO (DLCO). Moreover, was inversely correlated with maximal V O 2off and maximal work rate. In contrast, exhibited a significant positive correlation with tau V O 2off. These results indicate that V O 2off kinetics during recovery is related to re-oxygenation of peripheral skeletal muscle evaluated by NIRS in patients with COPD. Therefore, NIRS may be a useful tool to estimate the impairment of cardiopulmonary responses and re-oxygenation of peripheral skeletal muscle during the immediate recovery phase after exercise in COPD patients.

Aged↗

PubMed2001

Reaction kinetics of protease with substrate phage. Kinetic model developed using stromelysin.

Peptide libraries generated using phage display have been widely applied to proteolytic enzymes for substrate selection and optimization, but the reaction kinetics between the enzyme and substrate phage are not well understood. Using a quantitative ELISA assay to monitor the disappearance of substrate, we have been able to follow the course of reaction between stromelysin, a metalloprotease, and its substrate phage. We found that under the proteolytic conditions where the enzyme was present in nanomolar concentration or higher, in excess over the substrate, the proteolysis of substrate phage was a single exponential event and the observed rate linear with respect to enzyme concentration. The enzyme concentration dependence could be described by pseudo first-order kinetic equations. Our data suggest that substrate binding is slow relative to the subsequent hydrolysis step, implying that the phage display selection process enriches clones that have high binding affinity to the protease, and the selection may not discriminate those of different chemical reactivity toward the enzyme. Considering that multiple substrate molecules may be present on a single phage particle, we regard the substrate phage reaction kinetic model as empirical. The validity of the model was ascertained when we successfully applied it to determine the binding affinity of a competitive inhibitor of stromelysin.

Animals↗

PubMed2006

Determining RuBisCO activation kinetics and other rate and equilibrium constants by simultaneous multiple non-linear regression of a kinetic model.

The forward and reverse rate constants involved in carbamylation, activation, carboxylation, and inhibition of D-ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) have been estimated by a new technique of simultaneous non-linear regression of a differential equation kinetic model to multiple experimental data. Parameters predicted by the model fitted to data from purified spinach enzyme in vitro included binding affinity constants for non-substrate CO2 and Mg2+ of 200+/-80 microM and 700+/-200 microM, respectively, as well as a turnover number (k(cat)) of 3.3+/-0.5 s(-1), a Michaelis half-saturation constant for carboxylation (K(M,C)) of 10+/-4 microM and a Michaelis constant for RuBP binding (K(M,RuBP)) of 1.5+/-0.5 microM. These and other constants agree well with previously measured values where they exist. The model is then used to show that slow inactivation of RuBisCO (fallover) in oxygen-free conditions at low concentrations of CO2 and Mg2+ is due to decarbamylation and binding of RuBP to uncarbamylated enzyme. In spite of RuBP binding more tightly to uncarbamylated enzyme than to the activated form, RuBisCO is activated at high concentrations of CO2 and Mg2+. This apparent paradox is resolved by considering activation kinetics and the fact that while RuBP binds tightly but slowly to uncarbamylated enzyme, it binds fast and loosely to activated enzyme. This modelling technique is presented as a new method for determining multiple kinetic data simultaneously from a limited experimental data set. The method can be used to compare the properties of RuBisCO from different species quickly and easily.

Carbon Dioxide↗

PubMedDate not supplied

Comparison of a modified urea kinetic model direct dialysis quantification and classic urea kinetic modeling.

In the classic urea kinetic model (UkM), the measurement of clearance (K) as a model input is onerous, and its result is higher than actual body clearance because of urea disequilibrium. Urea kinetics performed by direct dialysis quantification (DDQ), with an equilibrated post rebound sample, gives reliable results but is routinely impractical. The modified UKM (mUKM) method is based on the input of urea distribution volume (V), easily obtainable by several methods and more stable than clearance, and uses simple formulae derived from urea mass balance, avoiding iterative computation. Compared with DDQ, mUKM results are identical, provided that the V value obtained by DDQ is used as input. Compared with UKM, mUKM urea clearances are significantly lower (158.1 +/- 20.5 versus 180.7 +/- 26.8 ml/min), as are urea nitrogen generation rates (5.85 +/- 2.0 versus 6.41 +/- 2.14 mg/min), whereas V results are close (32,444 +/- 6301 versus 32,141 +/- 5293 ml): consequently, mUKM Kt/V is significantly lower than UKM Kt/V (1.07 +/- 0.17 versus 1.22 +/- 0.18). This is because both mUKM and DDQ take account of post dialysis urea rebound. Therefore, if UKM formulae are used with the DDQ body clearance and the equilibrated post rebound blood urea nitrogen value as input data, their results strictly approximate the reference DDQ (V = 32,457 +/- 6274; Kt/V = 1.07 +/- 0.17; G = 5.85 +/- 2.0), demonstrating the common mathematical basis of DDQ and UKM. Therefore, reliable results may be obtained by DDQ, by mUKM, and by "equilibrated" UKM; we suggest that the mUKM model, less cumbersome than DDQ, and more reliable than UKM because it avoids the clearance measurement and the need for iterative computation, could be useful for routine kinetics.

Blood Urea Nitrogen↗

PubMed1982

Epithelial cells kinetics. A review of methods of study and their application to oral mucosa in health and disease. Part B. Comparison of cell kinetics in normal and abnormal epithelia.

In Part A, the techniques most commonly used to study epithelial cell kinetics and their suitability for use in man are reviewed. In Part B, the application of such methods to comparative studies of normal and abnormal oral epithelial of both man and experimental animals is examined. Claims regarding the possible prognostic value of LI's or MI's of biopsies of potentially or overtly malignant human oral lesions are also considered. Normal and abnormal kinetic data for other lining epithelia, e.g., skin, uterine cervix and gastrointestinal mucosa are assessed where they provide a better illustration of some of the problems arising in such comparative investigations. Finally, the present and likely future areas in which cell kinetic studies may provide a guide to expected tumour prognosis and optimum treatment are summarized.

Animals↗

PubMed2006

Quantitative analysis of the experimental O-J-I-P chlorophyll fluorescence induction kinetics. Apparent activation energy and origin of each kinetic step.

Fluorescence induction has been studied for a long time, but there are still questions concerning what the O-J-I-P kinetic steps represent. Most studies agree that the O-J rise is related to photosystem II primary acceptor (Q(A)) reduction, but several contradictory theories exist for the J-I and I-P rises. One problem with fluorescence induction analysis is that most work done to date has used only qualitative or semiquantitative data analysis by visually comparing traces to observe the effects of different chemicals or treatments. Although this method is useful to observe major changes, a quantitative method must be used to detect more subtle, yet important, differences in the fluorescence induction trace. To achieve this, we used a relatively simple mathematical approach to extract the amplitudes and half-times of the three major fluorescence induction phases obtained from traces measured in thylakoid membranes kept at various temperatures. Apparent activation energies (E(A)) were also obtained for each kinetic step. Our results show that each phase has a different E(A), with E(A O-J) <E(A J-I) < E(A I-P), and thus a different origin. The effects of two well-known chemicals, 3-(3,4-dichlorophenyl)-1,1-dimethylurea, which blocks electron transfer to the photosystem II secondary electron acceptor (Q(B)), and decylplastoquinone, which acts similarly to endogenous reducible plastoquinones, on the quantitative parameters are discussed in terms of the origin of each kinetic phase.

Algorithms↗

PubMed2005

Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: analysis of stopped-flow kinetic experiments.

Two fundamentally different mechanisms of ligand binding are commonly encountered in biological kinetics. One mechanism is a sequential multistep reaction in which the bimolecular binding step is followed by first-order steps. The other mechanism includes the conformational transition of the macromolecule, before the ligand binding, followed by the ligand binding process to one of the conformational states. In stopped-flow kinetic studies, the reaction mechanism is established by examining the behavior of relaxation times and amplitudes as a function of the reactant concentrations. A major diagnostic tool for detecting the presence of a conformational equilibrium of the macromolecule, before the ligand binding, is the decreasing value of one of the reciprocal relaxation times with the increasing [ligand]. The sequential mechanism cannot generate this behavior for any of the relaxation times. Such dependence is intuitively understood on the basis of approximate expressions for the relaxation times that can be comprehensively derived, using the characteristic equation of the coefficient matrix and polynomial theory. Generally, however, the used approximations may not be fulfilled. On the other hand, the two kinetic mechanisms can always be distinguished, using the approach based on the combined application of pseudo-first-order conditions, with respect to the ligand and the macromolecule. The two experimental conditions differ profoundly in the extent of the effect of the ligand on the protein conformational equilibrium. In a large excess of the ligand, the conformational equilibrium of the macromolecule, before the ligand binding, is strongly affected by the binding process. However, in a large excess of the macromolecule, ligand binding does not perturb the internal equilibrium of the macromolecule. As a result, the normal mode, affected by the conformational transition, is absent in the observed relaxation process. In the case of a sequential mechanism, the number of relaxation times is not altered by different pseudo-first-order conditions. Thus, the approach provides a strong diagnostic criterion for detecting the presence of the conformational transition of the macromolecule and establishing the correct mechanism. Application of this approach is illustrated for the binding of 3'-O-(N-methylantraniloyl)-5'-diphosphate to the E. coli DnaC protein.

Adenosine Diphosphate↗

PubMed1999

Suicide inactivation of peroxidase by H2O2: kinetic equations for peroxidatic oxidation reaction of guaiacol and determination of the kinetic parameters.

The kinetics of horseradish peroxidase (HRP) in oxidation reaction of guaiacol (AH) by hydrogen peroxide was studied, taking into account the inactivation of enzyme during reaction by its suicide substrate, H2O2. Those ranges of concentrations were selected in which: 1) the reaction was first-order in relation to [AH] and 2) [H2O2] >> [AH]. By combination of rate equations of the two concurrent reactions, consumption of AH and suicide inactivation of HRP, the overall kinetic equations were obtained which define the progress curve of reactions. The compatibility between equations and kinetic behaviour of reaction were evaluated in different ways. A close match was found between equations and experimental data. These equations can be used for determining 1) intact value of enzyme activity at start time of reaction and 2) apparent rate constant of suicide inactivation (ki') in a given concentration of H2O2, by processing of the data of the progress curve. The ki' value was found to be 0.178 +/- 0.003 min.-1 at 10 mM of H2O2 and 0.04 +/- 0.002 at 3 mM H2O2, at 27 degrees C and sodium phosphate buffer, pH = 7.0.

Enzyme Inhibitors↗

PubMed1999

Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: in vivo kinetic characterization of 2,3-bisphosphoglycerate synthase/phosphatase using 13C and 31P NMR.

This is the first in a series of three papers [see also Mulquiney and Kuchel (1999) Biochem. J. 342, 579-594; Mulquiney and Kuchel (1999) Biochem. J. 342, 595-602] that present a detailed mathematical model of erythrocyte metabolism which explains the regulation and control of 2,3-bisphosphoglycerate (2,3-BPG) metabolism. 2,3-BPG is a modulator of haemoglobin oxygen affinity and hence plays an important role in blood oxygen transport and delivery. This paper presents an in vivo kinetic characterization of 2,3-BPG synthase/phosphatase (BPGS/P), the enzyme that catalyses both the synthesis and degradation of 2,3-BPG. Much previous work had indicated that the behaviour of this enzyme in vitro is markedly different from that in vivo. (13)C and (31)P NMR were used to monitor the time courses of selected metabolites when erythrocytes were incubated with or without [U-(13)C]glucose. Simulations of the experimental time courses were then made. By iteratively changing the parameters of the BPGS/P part of the model until a good match between the NMR-derived data and simulations were achieved, it was possible to characterize BPGS/P kinetically in vivo. This work revealed that: (1) the pH-dependence of the synthase activity results largely from a strong co-operative inhibition of the synthase activity by protons; (2) 3-phosphoglycerate and 2-phosphoglycerate are much weaker inhibitors of 2,3-BPG phosphatase in vivo than in vitro; (3) the K(m) of BPGS/P for 2,3-BPG is significantly higher than that measured in vitro; (4) the maximal activity of the phosphatase in vivo is approximately twice that in vitro, when P(i) is the sole activator (second substrate); and (5) 2-phosphoglycollate appears to play no role in the activation of the phosphatase in vivo. Using the newly determined kinetic parameters, the percentage of glycolytic carbon flux that passes through the 2, 3-BPG shunt in the normal in vivo steady state was estimated to be 19%.

2,3-Diphosphoglycerate↗

PubMed2003

[Natural history of non specific neuralgias of the limbs. Exponential kinetics of the root pain recovery in sciatica and femoral neuralgia; uncertain kinetics for brachial neuralgia].

Very few studies are dedicated to the natural history of sciatica, and none to femoral neuralgia or brachial neuralgia natural course. Hence, the results of a collection of five studies on these topics appear worth being published. A rheumatology department. The first study was a retrospective comparison of sciatica (145 patients) and femoral neuralgia (63 patients). The second study was a retrospective study concerning 107 patients with sciatica observed in a second different period. A third and a fourth retrospective studies were carried out on 38 femoral neuralgia and 69 brachial neuralgia patients. The fifth study was a prospective cohort study on patients with sciatica. As there are no diagnosis criteria for non specific neuralgias, the diagnosis was based on seniors' opinion. Neuralgia due to specific causes were carefully excluded. As there are no relevant outcomes measures specially dedicated to idiopathic acute root pain, the full recovery of root pain was used as endpoint. The kinetics of sciatica and of femoral neuralgia recoveries are related Plotted as neuralgia survival sciatica as well as femoral neuralgia exhibited a decreasing, exponential kinetics curve. Half sciatica disappear each 6 to 7 weeks. Half femoral neuralgia disappear each 5 to 6 weeks. The brachial neuralgia survival exhibited a more complex kinetics. These pilot studies, do not allow definitive conclusions. Nevertheless, given the scarcity of available data, they may be used as a factual basis for perfectly designed prospective inception cohort studies.

Adolescent↗

PubMedDate not supplied

Mechanisms of lidocaine kinetics in the isolated perfused rat liver. II. Kinetics of steady state elimination.

The steady state kinetics of lidocaine and its metabolites were modeled using nonlinear elimination pathways for multiple enzymes. The main metabolites, monoethylglycinexylidide and 3-hydroxy-lidocaine, were infused in the absence of lidocaine to measure the kinetic parameters for secondary elimination. Data from continuous perfusion of lidocaine in the isolated perfused rat liver at concentrations ranging from 9.6 to 278 microM (N = 16) were used to calculate the kinetic parameters for formation of the main metabolites. The elimination of lidocaine in the liver was approximated by the well stirred model. The whole liver study gave higher elimination rates than were predicted from microsomal studies. The major pathways for elimination of lidocaine in the rat were deethylation and hydroxylation, and subsequent elimination along these pathways accounted for the poor material balance at low dosage levels. The observed competitive inhibition of hydroxylation was in agreement with the predictions of the model.

Animals↗

PubMed1988

Chymotrypsin-catalyzed peptide synthesis. Kinetic analysis of the kinetically controlled peptide-bond formation.

The kinetics of peptide-bond formation catalyzed by delta-chymotrypsin has been studied for a number of peptide products of different length using fixed concentrations of the acyl component (Ac-Phe-OMe, Ac-Ala-Ala-Phe-OMe, or Ac-Ala-Ala-Tyr-OMe) and varying concentration of the amino component (H-Ala-NH2 or H-Ala-Ala-NH2). The time course of the reactions was followed by monitoring ester consumption and peptide product formation by analytical HPLC. On the basis of a plausible four-centre mechanistic model, the theoretical time course of these reactions was calculated using rate and equilibrium constants determined by separate kinetic experiments. The excellent agreement observed between the theoretical and the experimental time courses supports the proposed mechanism and provides evidence for the validity of the present kinetic approach. By focusing attention on the rate constants which are critical for efficient synthesis, this mechanistic information constitutes a valuable basis for the use of the enzymatic peptide synthesis in preparative applications.

Chymotrypsin↗

PubMed1979

[Kinetics and load distribution of supported free-end prostheses. IV. Effect of the saddle curvature on the saddle resp. abutment kinetics and the load distribution in prosthesis beds without abutments].

The influence of the saddle curvature on abutment tooth kinetics and abutment tooth stress was studied with unilateral rigid and movable free-end saddle dentures. The results showed that, independent of the length of the saddle and/or of the saddle curvature, considerable horizontal and vertical extrusive abutment tooth stress is present in addition to vertical intrusive abutment tooth stress. The saddle kinetics are basically influenced by the form of the saddle. The kinetics cannot be altered appreciably because of the mechanical characteristics of the connecting elements; it can only be surpressed at the cost of increased pier stress.

Biomechanical Phenomena↗

PubMed1996

[Integral kinetics of multisubstrate enzyme reactions. Criteria of kinetic behavior and characteristic coordinates for solution of direct and reverse problems].

General schemes of unbranched multisubstrate enzyme reactions associated with enzyme inactivation during catalysis are analyzed. Equations of integral kinetics at constant substrate concentrations and at depletion in one of the substrate are presented. Experimental dose-response curve characterized by additivity of some enzyme intermediates (absorption spectra, fluorescence, EPR, etc.) are theoretically analyzed. Also rapid equilibrium at certain stages of enzyme reaction is considered. The interrelationship of enzyme intermediates is a criterion of the kinetic behavior of enzyme reaction mechanism. New coordinates are suggested for the analysis of the integral kinetics of self-inactivating enzymes. Results of the analysis are used for interpretation of the data on arachidonic cascade enzymes.

Animals↗

PubMed1997

The kinetic characteristics of L-type calcium channels in cardiac cells of hibernators. 2. Analysis of the kinetic model.

The present paper describes the experimental and theoretical investigations of the kinetic characteristics of the L-type Ca2+ channels in ground squirrels Citellus undulatus in two different physiological states (hibernation and spontaneous arousal). The perforated patch-clamp method was used in the experiments. We have shown in the previous study [1] that Ca2+ currents in hibernating and active animals may be described by the d2f1(2)f2 model. Based on that model, in this paper we studied in detail the main steps of the conductance regulation of Ca2+ channels: activation (d), slow (f1-type) and fast (f2-type) inactivations of the channel. Activation is related to the movement of the gating charge. Slow inactivation is associated with the movement of the gating charge and is current-dependent. Fast inactivation is a more complex process and cannot be represented as a single-stage conformational transition induced by the gating charge movement. It is regulated by cAMP phosphorylation. The differences in the Ca2+ current kinetics are observed virtually for all the components. In hibernating animals, the most pronounced shift (15-20 mV) towards depolarization is experienced by the normalized conductances of both inactivation components, whereas the conductance of the activation component is shifted to a lesser extent. The characteristic times of Ca2+ currents of hibernating ground squirrels are 1.5-2 times greater than those of aroused animals. The current activation gating charge of Ca2+ channels in ground squirrel cardiocytes was found to change. The gating charge was about 2 in hibernating animals and 1.5 in active squirrels. The effect of isoproterenol-induced cAMP-dependent phosphorylation on Ca2+ currents in cardiocytes from hibernating ground squirrels was studied. Isoproterenol restored the kinetic parameters of Ca2+ currents to the values close to the parameters of active animals. However, we failed to explain the suppression of the Ca2+ current in hibernating animals in terms of cAMP-dependent regulation only.

Animals↗

PubMed1984

Isomer identification by kinetic energy release measurements using the voltage pulsed collision cell technique in mass-analysed ion kinetic energy spectrometry.

The voltage pulsing of the collision cell on a mass-analysed ion kinetic energy spectrometer allows simultaneous kinetic energy release measurements for unimolecular (T(V)), collision-induced (TCID(V)) and composite unimolecular and collision-induced (Tcomp(V)) decomposition processes in the time frame of a capillary gas chromatographic peak. The information gained by voltage pulsing sometimes allows more reliable isomer identification than by kinetic energy release measurements made in the non-pulsing mode alone. Presented are T(V), TCID(V) and Tcomp(V), and the ratio of their intensities for a number of isomeric halogenated compounds.

Hydrocarbons, Halogenated↗

PubMed2004

Does alpha-fluorination affect the structural trans-influence and kinetic trans-effect of an alkyl ligand? Molecular structures of Pd(TMEDA)(CH(3))(R(F)) and a kinetic study of the trans to cis isomerization of Pt(TMEDA)(CH(3))(2)I(R(F)) [R(F) = CF(2)CF(3), CFHCF(3), CH(2)CF(3)].

Reaction of Pd(TMEDA)(CH(3))(2) [TMEDA = tetramethylethylenediamine] with fluoroalkyl iodides R(F)I affords a series of square planar Pd(II) complexes Pd(TMEDA)(CH(3))(R(F)) [R(F) = CF(2)CF(3) (9), CFHCF(3) (10), CH(2)CF(3) (11)], presumably by oxidative addition followed by reductive elimination of CH(3)I. The solid-state structures of each compound have been determined by single crystal X-ray diffraction studies, allowing the effect of increasing alpha-fluorination on the structural trans-influence of alkyl ligands to be examined. In these compounds there is no significant difference observed in the trans-influence of the three fluorinated alkyl ligands toward the trans-N atom, although a significant cis-influence on the neighboring methyl ligand is apparent. Oxidative addition of the same series of fluoroalkyl ligands to the corresponding Pt(TMEDA)(CH(3))(2) affords octahedral Pt(IV) complexes trans-Pt(TMEDA)(CH(3))(2)(R(F))I [R(F) = CF(2)CF(3) (12), CFHCF(3) (13), CH(2)CF(3) (14)] as the kinetic products. In each case, subsequent isomerization to the corresponding all cis-isomers is observed; in the case of 13, the stereocenter at the alpha-carbon results in two diastereomeric cis-isomers, which are formed at different rates. The molecular structures of 13 and its more stable all cis-isomer 16b have been crystallographically determined. Kinetic studies of the trans-cis isomerization reactions show the mechanism to involve a polar transition state, presumably involving iodide dissociation, followed by rearrangement of the cation, and iodide recombination. High dielectric solvents increase the rate, but solvent coordinating ability has no effect. Dissolved salts (LiI, LiOTf) show normal accelerative salt effects, with no inhibition in the case of added iodide, consistent with the formation of an intimate ion pair intermediate. The kinetic parameters show that the trans-effects of fluoroalkyl ligands in these compounds follow the order expected from the relative sigma-donor properties of the ligands, with CF(2)CF(3) < CFHCF(3) < CH(2)CF(3).

Journal Article↗

PubMed2001

Kinetic studies of Heck coupling reactions using palladacycle catalysts: experimental and kinetic modeling of the role of dimer species.

Experimental kinetic studies of the coupling of p-bromobenzaldehyde (1) with butyl acrylate (2) using the dimeric palladacycles complex (4) with chelating nitrogen ligands were carried out together with kinetic modeling using a reaction rate expression based on the mechanism shown in Scheme 2. The oxidative addition product of 1 was found to be the resting state within the catalytic cycle. The formation of dimeric Pd species external to the catalytic cycle helped to rationalize a non-first-order rate dependence on catalyst concentration. Theoretical modeling showed how the relative concentrations of the different intermediate species within the catalystic cycle can influence the observed rate dependence on Pd concentration. It was shown how conventional kinetic studies may give reaction orders in substrates which differ from those which would be observed under practical synthetic conditions. Comparison between phosphine- and nonphosphine-based palladacycles suggests that they follow the same reaction mechanism. The role of water in accelerating the initial formation of the active catalyst species is noted.

Journal Article↗