In situ perpetual regeneration of a Ni-faujasite methanation catalyst

Jaeger, N. I.; Schulz‐Ekloff, G.; Kapička, Jiří

doi:10.1007/bf00769671

Cited by 4 publications

(2 citation statements)

References 11 publications

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“…This is especially true for a class of “switchable” proteins that has multiple populated conformational states. Lipase is one such important protein which is activated at a water–oil immiscible interface . It can serve as a model system to study a class of important, yet unexplored, interfacial proteins that function at biological interfaces (such as the surface of lipid droplets) …”

Section: Introductionmentioning

confidence: 99%

Pressure‐induced conformational switch of an interfacial protein

et al. 2016

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A special class of proteins adopts an inactive conformation in aqueous solution and activates at an interface (such as the surface of lipid droplet) by switching their conformations. Lipase, an essential enzyme for breaking down lipids, serves as a model system for studying such interfacial proteins. The underlying conformational switch of lipase induced by solvent condition is achieved through changing the status of the gated substrate-access channel. Interestingly, a lipase was also reported to exhibit pressure activation, which indicates it is drastically active at high hydrostatic pressure. To unravel the molecular mechanism of this unusual phenomenon, we examined the structural changes induced by high hydrostatic pressures (up to 1500 MPa) using molecular dynamics simulations. By monitoring the width of the access channel, we found that the protein undergoes a conformational transition and opens the access channel at high pressures (>100 MPa). Particularly, a disordered amphiphilic α5 region of the protein becomes ordered at high pressure. This positive correlation between the channel opening and α5 ordering is consistent with the early findings of the gating motion in the presence of a water-oil interface. Statistical analysis of the ensemble of conformations also reveals the essential collective motions of the protein and how these motions contribute to gating. Arguments are presented as to why heightened sensitivity to high-pressure perturbation can be a general feature of switchable interfacial proteins. Further mutations are also suggested to validate our observations. Proteins 2016; 84:820-827. © 2016 Wiley Periodicals, Inc.

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Section: Introductionmentioning

confidence: 99%

Pressure‐induced conformational switch of an interfacial protein

et al. 2016

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“…Some authors have reported results of FTIR absorption of CO on zeolites modified with platinum. For example Jaeger and Schulz-Eldoff [49] have speculated about the existence of two types of Pt particles on Pt/KL zeolite catalysts. The first one would be localized on the outer surface of the zeolite microcrystals or at near surface locations.…”

Section: Catalystmentioning

confidence: 99%