Transient kinetics of flavin-photosensitized oxidation of reduced redox proteins. Comparison of c-type cytochromes and plastocyanins
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1991.tb16115.x/fullpdf
Reference18 articles.
1. Flavin-photosensitized oxidation of reduced c-type cytochromes. Reaction mechanism and comparison with photoreduction of oxidized cytochromes by flavin semiquinones
2. Elucidation of the factors which determine reaction-rate constants and biological specificity for electron-transfer proteins
3. Electron transfer in biology. The function of cytochrome c
4. The effect of ethylenediamine chemical modification of plastocyanin on the rate of cytochrome f oxidation and P-700+ reduction
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2. Diversity of Interactions in Redox Systems: From Short- to Long-Lived Complexes;Redox Proteins in Supercomplexes and Signalosomes;2015-10-15
3. Probing the reactivity of different forms of azurin by flavin photoreduction;FEBS Journal;2011-03-22
4. Dynamic Ionic Strength Effects in Fast Bimolecular Electron Transfer between a Redox Metalloprotein of High Electrostatic Charge and an Inorganic Reaction Partner;The Journal of Physical Chemistry B;2000-11-10
5. Photosensitized electron transfer reactions of cytochrome c4 from Pseudomonas stutzeri with flavins and methyl viologen;Inorganica Chimica Acta;1998-05
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