2009
DOI: 10.1016/j.bbabio.2009.01.016
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Characterisation of the electron transfer and complex formation between Flavodoxin from D. vulgaris and the haem domain of Cytochrome P450 BM3 from B. megaterium

Abstract: Investigation of the complex formation and electron transfer kinetics between P450 BMP and flavodoxin was carried out following the suggested involvement of flavodoxin in modulating the electron transfer to BMP in artificial redox chains bound to an electrode surface. While electron transfer measurements show the formation of a tightly bound complex, the NMR data indicate the formation of shortly lived complexes. The measured k(obs) ranged from 24.2 s(-1) to 44.1 s(-1) with k(on) ranging from 0.07 x 10(6) to 1… Show more

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Cited by 6 publications
(7 citation statements)
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“…This inference is consistent with the observation of two different types of complexes of rabbit microsomal cytochrome P450 2B4 with CPR, only one of which is governed by electrostatic interactions, whereas the second contact region is hydrophobic [59]. Our observation is also consistent with the recent indication of multiple orientations of the flavoprotein in the complexes of the heme domain of P450BM-3 with the flavodoxin from Desulfovibrio vulgaris (which served as a model of the FMN domain of BMR) [60]. …”
Section: Discussionsupporting
confidence: 92%
“…This inference is consistent with the observation of two different types of complexes of rabbit microsomal cytochrome P450 2B4 with CPR, only one of which is governed by electrostatic interactions, whereas the second contact region is hydrophobic [59]. Our observation is also consistent with the recent indication of multiple orientations of the flavoprotein in the complexes of the heme domain of P450BM-3 with the flavodoxin from Desulfovibrio vulgaris (which served as a model of the FMN domain of BMR) [60]. …”
Section: Discussionsupporting
confidence: 92%
“…Electron transfer rates doubled in a flavodoxin/BMP construct as KCl concentrations were raised from 50 mM to 250 mM, for instance, underpinned by a significant tightening in binding between the two proteins, but then decreased on a further increase to 400 mM. 230,231 It was postulated that constructive reorganisation of the electrostatic complex accounted for the initial response, but that dissociation took place when ionic strength became excessive, as observed with other redox partner systems. 231 The N-demethylation of erythromycin by three separate fusions also displayed ionic strength-dependence across the 0-500 mM NaCl concentration range, peaking at 500 mM.…”
Section: Effectors Competitive Binding and Allosteric Regulationmentioning
confidence: 99%
“…230,231 It was postulated that constructive reorganisation of the electrostatic complex accounted for the initial response, but that dissociation took place when ionic strength became excessive, as observed with other redox partner systems. 231 The N-demethylation of erythromycin by three separate fusions also displayed ionic strength-dependence across the 0-500 mM NaCl concentration range, peaking at 500 mM. 189 Kinetic titrations with palmitic acid became sigmoidal as ionic strength was reduced, the point at which Michaelis-Menten kinetics ceased to apply being higher in Tris/HCl (50 mM) than in phosphate (25 mM).…”
Section: Effectors Competitive Binding and Allosteric Regulationmentioning
confidence: 99%
See 1 more Smart Citation
“…BiGGER has been used in the last decade to obtain structural models of several electron transfer and proteinprotein complexes [8][9][10], in most cases when the threedimensional structures of the proteins involved are available and the residues at the interface are either not known or known only for one of the partners. Although the coordinates used are considered as ''rigid bodies'', the algorithm offers an option called ''soft-docking'' that takes into account the conformational freedom of some of the surface residue side chains, such as lysine, to assist the prediction of the mode of binding of the two proteins.…”
Section: Introductionmentioning
confidence: 99%