Croatica Chemica Acta, Vol. 49 No. 2, 1977.
Conference paper
Low Temperature Kinetics as a Probe of Protein Structure and Dynamics
R. H. Austin
; Max Planck Institute for Biophysical Chemistry, Gottingen-Nikolausberg, Federal Republic of Germany
Abstract
The recombination kinetics of flash-photolyzed carbon monoxy
heme proteins has been studied as a function of temperature over
the range of 2 K-350 K. Low temperature kinetics (< 200 K) reveal
that internal activation energy barriers to recombination (a) control
the room temperature kinetics, (b) are of a distributed nature, forming
an ensemble of activation energies, (c) are specific to the
protein studied and are sensitive to the presence of substrates
bound to the protein.
Cytochrome P450 from camphor induced Pseudomonas putida
reveals low temperature kinetics which are highly dependent on the
presence or absence of the camphor substrate.
Keywords
Hrčak ID:
196368
URI
Publication date:
30.3.1977.
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