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Title: Electron transport networks in multicentre metalloproteins
Authors: Christensen, H.E.M. 
Coutinho, I.
Conrad, L.S.
Hammerstad-Pedersen, J.M.
Iversen, G.
Jensen, M.H.
Karlsson, J.J.
Ulstrup, J.
Xavier, A.V.
Issue Date: 23-Aug-1994
Citation: Christensen, H.E.M.,Coutinho, I.,Conrad, L.S.,Hammerstad-Pedersen, J.M.,Iversen, G.,Jensen, M.H.,Karlsson, J.J.,Ulstrup, J.,Xavier, A.V. (1994-08-23). Electron transport networks in multicentre metalloproteins. Journal of Photochemistry and Photobiology, A: Chemistry 82 (1-3) : 103-115. ScholarBank@NUS Repository.
Abstract: Electron transfer (ET) in multicentre proteins exhibits cooperativity, i.e. mutual electrostatic, spectral, and structural interactions between the individual ET centres. We investigate here two kinds of cooperativity. The first is "static" and is represented by the electrostatic interaction between two charged centres inside or outside a solvated dielectric globule. Such effects can be the origin of interaction reduction potentials and also provide a basis for calculation of the protein and solvent reorganization Gibbs energy of intramolecular ET. Cooperativity effects in the second class are "dynamic" and originate from partial vibrational relaxation of intermediate states in multistep ET. This leads to coherence in the ET sequence. The concepts and formalism are applied to the ET patterns of the two-heme cytochrome c4, four-heme cytochrome c3, and the bacterial photosynthetic reaction centre. It is shown that cooperativity in the approximately thermoneutral ET steps of the cytochromes is likely to be "static" while the activationless nature of the photosynthetic ET steps can also lead to coherence in the overall ET sequence. © 1994.
Source Title: Journal of Photochemistry and Photobiology, A: Chemistry
ISSN: 10106030
Appears in Collections:Staff Publications

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