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• W2009289498 abstract "Abstract The first section of this paper is a detailed summary of studies made by us and others on metal cations binding to deionized bacteriorhodopsin (dIbR) and its variants. Our studies include the luminescence experiments of Eu 3+ binding to dIbR and potentiometric studies of Ca 2+ binding to dIbR, to deionized bR mutants, to bacterioopsin, and to dIbR with its C‐terminus removed. The results suggest the presence of two classes of binding sites, one class has two high‐affinity constants, and one has one low‐affinity constant. For Ca 2+ binding, there is one metal cation in each of the two high‐affinity sites which are coupled to the charged aspartates 85 and 212 (known to be in the retinal cavity) but not coupled to each other. The low‐affinity class can accommodate 0–6 Ca 2+ ions and most of them are bound to the surface. Mg 2+ has a slightly smaller value for its binding constant to the highest‐affinity site. Thus, one expects more Ca 2+ than Mg 2+ bound to the two high‐affinity sites. In the second section, we summarize our recent study on the effect of metal cation charge density (Ca 2+ , Mg 2+ , Eu 3+ , Tb 3+ , Ho 3+ , Dy 3+ ) on the kinetics of both Schiff base deprotonation and proton transport to the extracellular surface. For all metal cations, the apparent rate constant of the slow components of the deprotonation process is the same as that for the transport process at 22 °C. The temperature studies, however, show this apparent equality to be fortuitous and to result from cancellation of the contribution of the energy and entropy of activation. Thus, while the entropy of activation is positive for the deprotonation process, it is negative for the proton transport process. These kinetic parameters depend weakly on the charge density, but in an opposite sense for the two processes. These results suggest that the deprotonation is not the rate‐limiting step for the proton transport process. A possible mechanism is proposed in which a hydrated metal cation is used to induce the deprotonation of the protonated Schiff base and to dissociate one of its H 2 O molecules to donate the proton in the L → M process." @default.
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• W2009289498 date "1995-01-01" @default.
• W2009289498 modified "2023-10-16" @default.
• W2009289498 title "The Effect of Different Metal Cation Binding on the Proton Pumping in Bacteriorhodopsin" @default.
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• W2009289498 doi "https://doi.org/10.1002/ijch.199500043" @default.
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