Distance-dependent electron transfer rate of immobilized redox proteins: A statistical physics approach
نویسندگان
چکیده
منابع مشابه
Factors influencing redox potentials of electron transfer proteins.
The redox potentials of electron transfer proteins vary over a wide range, even when the type of redox center is the same. Rees [Proc. Natl. Acad. Sci. USA (1985) 82, 3082-3085] proposed that this variation of redox potential partly reflects the different net charges of the proteins, and he presented a linear correlation between these two properties for 36 proteins. A review of the factors that...
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A theoretical model describing the transport and kinetic processes involved in heterogeneous redox catalysis of solution phase reactants at electrode surfaces coated with redox active monolayers is presented. We describe theoretically the time dependent chronoamperometric response expected for a redox active monolayer in the absence of a substrate in solution, and subsequently extend the analys...
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4.3. Variability in cytochrome groups. . . . . . . . . . . . . . 4.4. List of cytochromes . . . . . . . . . . . . . . . . . . . . . . 4.4.1. Cytochrome-a group . . . . . . . . . . . . . . . . . 4.4.2. Cytochrome-b group . . . . . . . . . . . . . . . . . 4.4.3. Cytochrome-c group . . . . . . . . . . . . . . . . . 4.4.4. Cytochrome-d group . . . . . . . . . . . . . . . . . 5. Non-heme iron protei...
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The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-bi...
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ژورنال
عنوان ژورنال: Physical Review E
سال: 2010
ISSN: 1539-3755,1550-2376
DOI: 10.1103/physreve.81.046101