Electron transfer kinetic model, flavocytochrome

Fig. 11. Molecular model and electron transfer kinetics of the flavocytochrome ma-quette containing two bis-histidine hgated hemes and two covalently bound flavins (149). Copyright 1998 National Academy of Sciences, USA.

Electron transfer (continued) intramolecular, from type-1 copper center to trinuclear copper center blue copper oxidases, 40 175-178 iron-sulfur proteins, 47 405, 474-479 kinetic model, flavocytochrome bj, 36 282-283... 

Fig 14. A kinetic model (123) of electron transfer in flavocytochrome 62- Each semicircle represents two of the four subunits of the enzyme during phase 1. Phase 1 corresponds to the entry of the first two electron pairs per dimer. After interprotomer electron transfer to give one fully reduced FMN and one flavosemiquinone, the dimer undergoes a conformation change (rectangles) to allow entry of the third electron pair per dimer (phase 2) to give fully reduced flavocytochrome 62. H, Heme F, FMN S, substrate P, product. 

Capeillere-Blandin, C. and Albani, J. 1987, Cytochrome b2, an electi on carrier between flavocytochrome b, and cytochrome c Rapid kinetic characterisation of the electron transfer parameters with ionic strength dependence. Biochemical Journal 245, 159-165. Carpita, N. C. and Gibeaut, D. M. 1993, Structural models of primary cell walls in flowering plants consistency of molecular structure with the physical properties of the walls during growth. Plant Journal 3, 1 -30. 

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