We have investigated the kinetics of ligand rebinding after nano-second laser photolysis of horse heart carboxymyoglobin, encapsulated in wet silica gels. The geminate ligand rebinding to the gel embedded protein shows a markedly enhanced efficiency, 0.43, with respect to solution. This geminate phase can be described by a stretched exponential decay. The second-order rate of CO rebinding to myoglobin (Mb) gels is View the MathML source. The bimolecular binding rate is thermally activated with barriers of approximately 4 kcal mol−1. These findings indicate that Mb within silica gels is in an environment with an apparent higher local viscosity than in solution.

Enhanced geminate ligand rebinding upon photo-dissociation of silica gels-embedded myoglobin-CO / ABBRUZZETTI S.; VIAPPIANI C.; BRUNO S.; MOZZARELLI A.. - In: CHEMICAL PHYSICS LETTERS. - ISSN 0009-2614. - 346(2001), pp. 430-436. [10.1016/s0009-2614(01)01027-2]

Enhanced geminate ligand rebinding upon photo-dissociation of silica gels-embedded myoglobin-CO

ABBRUZZETTI, Stefania;VIAPPIANI, Cristiano;BRUNO, Stefano;MOZZARELLI, Andrea
2001

Abstract

We have investigated the kinetics of ligand rebinding after nano-second laser photolysis of horse heart carboxymyoglobin, encapsulated in wet silica gels. The geminate ligand rebinding to the gel embedded protein shows a markedly enhanced efficiency, 0.43, with respect to solution. This geminate phase can be described by a stretched exponential decay. The second-order rate of CO rebinding to myoglobin (Mb) gels is View the MathML source. The bimolecular binding rate is thermally activated with barriers of approximately 4 kcal mol−1. These findings indicate that Mb within silica gels is in an environment with an apparent higher local viscosity than in solution.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11381/1458086
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