The Influence of the Net Protein Charge on the Rate of Formation of Enzyme–Substrate Complexes.

Hammes, Gordon G.; Alberty, Robert A.

doi:10.1021/j150572a034

Cited by 35 publications

(11 citation statements)

References 4 publications

(7 reference statements)

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“…Although high, such a value is quite possible in view of the investigation by Alberty & Hammes (1958) of the rate at which a diffusion-controlled reaction can take place with a specific site freely accessible from all points in a hemisphere. The effect of decreasing the salt concentration on the ratio k2/k1 (Table 3) is also in the direction to be expected from the later investigation of Hammes & Alberty (1959) of electrostatic effects in such reactions. Similarly, the effect of 60 % sucrose on the reaction may be explained by supposing that k, is much reduced by the increase in viscosity.…”

Section: Compari8on Of Theory and Experimentssupporting

confidence: 52%

Kinetic studies on the reaction between native globin and haem derivatives

Gibson

Antonini

1960

Biochemical Journal

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It was reported by Hill & Holden (1926), and confirmed by later workers, that the reaction between haematin and globin is rapid, but no numerical results appear to have been published. The reaction between peroxidase apoprotein and haematin has, however, been examined (Theorell & Maehly, 1950). It was slow, with a half-time of the order of minutes; the results with different preparations showed variations up to seven-fold in the rate.

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Section: Compari8on Of Theory and Experimentssupporting

confidence: 52%

Kinetic studies on the reaction between native globin and haem derivatives

Gibson

Antonini

1960

Biochemical Journal

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“…For both N-SOD and PEG-SOD the trends of k versus I appear to be in agreement with the ones predicted by Alberty and Hammes (Alberty and Hammes, 1958;Hammes and Alberty, 1959;Argese et al, 1987).…”

Section: Results and Discussion Comparison Between Kinetic Behaviourssupporting

confidence: 84%

Comparative kinetic study between native and chemically modified Cu,Zn superoxide dismutases

Argese

Girotto

Orsega

1993

Biochemical Journal

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The kinetic behaviour of native bovine erythrocyte Cu,Zn superoxide dismutase (N-SOD) and of its derivatives by reaction with polyethylene glycol, acetic and succinic anhydrides has been investigated here in detail. Their responses to changes of pH and ionic strength (I) have been used as a probe for quantitatively displaying the relevance to kinetic rate constant of superficial positive charges driving the superoxide ion (O2-) toward the enzyme's active site. Overall kinetic trends indicate that this long-range O2- electrostatic guidance is essentially due to the positive charges of the amino-acid residues Lys-120 and Lys-134 which are strategically located around the active site. The comparison between the kinetic data obtained from N-SOD and those from polyethylene-glycolated SOD (PEG-SOD) enabled us to state that in PEG-SOD an O2(-)-steering positive electrostatic force, halved in comparison with N-SOD, is still operating, and that only Lys-120 is linked in the reaction of N-SOD with PEG. Elimination of the electrostatic driving force, carried out either by deprotonation of lysine amino groups at high pH, or by their neutralization with succinic anhydride and acetic anhydride, or by ionic screening at high ionic strength, always lowered the kinetic rate constant to a value of approx. 3 x 10(8) M-1.s-1. This value is about 15 times smaller than that measured in the presence of the reactant-steering mechanism and represents the k value of the reaction limited by pure diffusion. Finally, the kinetic behaviour of acetylated SOD and succinylated SOD demonstrated the inhibitor effect of OH- at strongly alkaline pH.

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“…(We choose to definef (r, t ro) so as to incorporate the angular factors of 27r[s = 2] and 4w(s = 3).) We shall assume that the radial propagator satisfies the Smoluchowski mean-field diffusion equation (7) -f(r, tIro) = r-' rs-rI D(r) [d + "'(r)'f(r, t'Iro) (4) at Olr [Or~r) 4…”

Section: Spb Equationmentioning

confidence: 99%

“…However, such work is crucial to the understanding of diffusion-controlled chemical kinetics and transport of ionic species in an immense variety of systems. In dealing with these problems, previous authors have either resorted to linear approximations and numerical solutions (3,4) or simply neglected many-body effects (screening) altogether (5,6).…”

Section: Introductionmentioning

confidence: 99%

The Smoluchowski-Poisson-Boltzmann description of ion diffusion at charged interfaces

Chan¹,

Halle²

1984

Biophysical Journal

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A theoretical description of ion diffusion in the electric field set up by the double layer in the neighborhood of a charged interface is presented. Such a description is needed for the understanding of diffusion-controlled chemical kinetics and transport of ionic species in a variety of systems of interest in biophysics, electrochemistry, and colloid science. The ion dynamics are taken to be governed by the Smoluchowski diffusion equation and the average electrostatic field is obtained from the nonlinear Poisson-Boltzmann equation. Diffusion in finite regions with partially absorbing boundaries of planar, cylindrical, or spherical geometry is considered. The complete analytical solution of the Smoluchowski-Poisson-Boltzmann equation for counterions between two planar charged interfaces is given. Simple expressions are derived for certain useful integral quantities, viz., mean absorption times and absorption probabilities, in all geometries considered. Finally, lateral counterion diffusion and its consequences for surface re-encounter-enhanced chemoreception is considered.

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The Influence of the Net Protein Charge on the Rate of Formation of Enzyme–Substrate Complexes.

Cited by 35 publications

References 4 publications

Kinetic studies on the reaction between native globin and haem derivatives

Kinetic studies on the reaction between native globin and haem derivatives

Comparative kinetic study between native and chemically modified Cu,Zn superoxide dismutases

The Smoluchowski-Poisson-Boltzmann description of ion diffusion at charged interfaces

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