Differential influence of dynamic processes on forward and reverse electron transfer across a protein-protein interface.
We propose that the forward and reverse halves of a flash-induced protein-protein electron transfer (ET) photocycle should exhibit differential responses to dynamic interconversion of configurations when the most stable configuration is not the most reactive, because the reactants exist in different initial configurations: the flash-photoinitiated forward ET process begins with the protein partners in an equilibrium ensemble of configurations, many of which have little or no reactivity, whereas the reactant of the thermal back ET (the charge-separated intermediate) is formed in a nonequilibrium, "activated" protein configuration. We report evidence for this proposal in measurements on (i) mixed-metal hemoglobin hybrids, (ii) the complex between cytochrome c peroxidase and cytochrome c, and (iii and iv) the complexes of myoglobin and isolated hemoglobin alpha-chains with cytochrome b(5). For all three systems, forward and reverse ET does respond differently to modulation of dynamic processes; further, the response to changes in viscosity is different for each system.
Hoffman
Brian M
BM
Department of Chemistry, Northwestern University, 2145 North Sheridan Road, Evanston, IL 60208-3113, USA. bmh@northwestern.edu
Celis
Laura M
LM
Cull
Deborah A
DA
Patel
Ami D
AD
Seifert
Jennifer L
JL
Wheeler
Korin E
KE
Wang
Jingyun
J
Yao
Jiang
J
Kurnikov
Igor V
IV
Nocek
Judith M
JM
D003578:Cytochrome-c Peroxidase / Q000737:chemistry; D045304:Cytochromes c / Q000737:chemistry; D004579:Electron Transport; D006454:Hemoglobins / Q000737:chemistry; D006801:Humans; D009211:Myoglobin / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014783:Viscosity
D006454:Hemoglobins; D009211:Myoglobin; D011506:Proteins; D045304:Cytochromes c; D003578:Cytochrome-c Peroxidase
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