The Complex of Cytochrome <i>f</i> and Plastocyanin from <i>Nostoc</i> sp. PCC 7119 is Highly Dynamic

Scanu, Sandra; Förster, Johannes; Finiguerra, Michela G.; Shabestari, Maryam Hashemi; Huber, Martina; Ubbink, Marcellus

doi:10.1002/cbic.201200073

Cited by 22 publications

(62 citation statements)

References 31 publications

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“…8 and 9, the relative small scale of overall chemical shift perturbations and the presence of affected residues that are distant from the FMN cofactor suggest the existence of an ensemble of dynamic complexes. Similar complexes were observed in a number of electron transfer protein systems, including cyt b 5 -cyt P450 (22,58), adrenodoxin-cyt c (44), myoglobin-cyt b 5 (23), cyt c-cyt b 5 (24,43), and plastocyanin-cyt f complexes (59). Dynamic complexes are usually formed between two proteins rich in complementary charges and dominantly driven by long-range electrostatic interactions (57).…”

Section: Comparison Of Cyt C Reduction By Fbd and Full-lengthsupporting

confidence: 52%

Kinetic and Structural Characterization of the Interaction between the FMN Binding Domain of Cytochrome P450 Reductase and Cytochrome c

Huang

Zhang

Rwere

et al. 2015

Journal of Biological Chemistry

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Section: Comparison Of Cyt C Reduction By Fbd and Full-lengthsupporting

confidence: 52%

Kinetic and Structural Characterization of the Interaction between the FMN Binding Domain of Cytochrome P450 Reductase and Cytochrome c

Huang

Zhang

Rwere

et al. 2015

Journal of Biological Chemistry

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“…The global fit of the binding curves to a 1:1 binding model yielded a dissociation constant of 4 (±1) × 10 −4 M. This value is in-between the reported values for the Ph-Ph complex and N−N complex, being ≈10 × 10 −4 M 21 and 0.8 × 10 −4 M, 27 respectively. Whereas the cross-complex formed by Ph Cyt f and N Pc ( Ph-N complex) was reported to have similar affinity to the N−N complex (K D = 0.8 × 10 −4 M), 25 the N-Ph complex shows an affinity intermediate to that of the two physiological complexes but closer to that of the Ph-Ph complex.…”

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confidence: 71%

Loss of Electrostatic Interactions Causes Increase of Dynamics within the Plastocyanin–Cytochrome f Complex

et al. 2013

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Recent studies on the electron transfer complex formed by cytochrome f and plastocyanin from Nostoc revealed that both hydrophobic and electrostatic interactions play a role in the process of complex formation. To study the balance between these two types of interactions in the encounter and the final state, the complex between plastocyanin from Phormidium laminosum and cytochrome f from Nostoc sp. PCC 7119 was investigated using NMR spectroscopy and Monte Carlo docking. Cytochrome f has a highly negative charge. Phormidium plastocyanin is similar to that from Nostoc, but the net charge of the protein is negative rather than positive. NMR titrations of Zn-substituted Phormidium plastocyanin and Nostoc cytochrome f indicated that a complex with an affinity intermediate between those of the Nostoc and Phormidium complexes is formed. Plastocyanin was found in a head-on orientation, as determined using pseudocontact shifts, similar to that in the Phormidium complex, in which the hydrophobic patch represents the main site of interaction on plastocyanin. However, the interaction in the cross-complex is dependent on electrostatics, similar to that in the Nostoc complex. The negative charge of plastocyanin decreases, but not abolishes, the attraction to cytochrome f, resulting in the formation of a more diffuse encounter complex than in the Nostoc case, as could be determined using paramagnetic relaxation spectroscopy. This work illustrates the subtle interplay of electrostatic and hydrophobic interactions in the formation of transient protein complexes. The results are discussed in the context of a model for association on the basis of hydrophobic contacts in the encounter state.

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“…-CLaNP-7 and MTSL were analyzed as reported before (10,24). Briefly, the peak heights of the amide resonances of the proteins in the presence of partner protein with either a diamagnetic probe (Lu where x is the vector of the weights of the N structures composing the considered pool of conformers; y is the vector of M experimentally observed values of PCSs, RDCs, and PREs normalized by their respective norms; and A is the M × N matrix with columns that contain the PCS, RDC, and PRE values back-calculated for each of the conformers (SI Text), again normalized by the norm of the experimental data.…”

Section: +mentioning

confidence: 99%

“…In the encounter complex, the proteins assume multiple other orientations, often in equilibrium with the major stereospecific state. In low-affinity complexes with dissociation constant (K d ) values > 10 μM, the encounter complex can represent a sizeable fraction, and in some cases, a well-defined, stereospecific complex may even be absent (10)(11)(12)(13)(14)(15). The presence of encounter states may be a consequence of the chemical nature of proteins.…”

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confidence: 99%

Identification of productive and futile encounters in an electron transfer protein complex

Andrałojć

Hiruma

Wei-min

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Well-defined, stereospecific states in protein complexes are often in exchange with an ensemble of more dynamic orientations: the encounter states. The structure of the stereospecific complex between cytochrome P450cam and putidaredoxin was solved recently by X-ray diffraction as well as paramagnetic NMR spectroscopy. Other than the stereospecific complex, the NMR data clearly show the presence of additional states in the complex in solution. In these encounter states, populated for a small percentage of the time, putidaredoxin assumes multiple orientations and samples a large part of the surface of cytochrome P450cam. To characterize the nature of the encounter states, an extensive paramagnetic NMR dataset has been analyzed using the Maximum Occurrence of Regions methodology. The analysis reveals the location and maximal spatial extent of the additional states needed to fully explain the NMR data. Under the assumption of sparsity of the size of the conformational ensemble, several minor states can be located quite precisely. The distribution of these minor states correlates with the electrostatic potential map around cytochrome P450cam. Whereas some minor states are on isolated positively charged patches, others are connected to the stereospecific site via positively charged paths. The existence of electrostatically favorable pathways between the stereospecific interaction site and the different minor states or lack thereof suggests a means to discriminate between productive and futile encounter states.paramagnetic NMR | encounter complex | cytochrome P450cam | putidaredoxin | maximum occurrence C rystal structures suggest that proteins assume unique, stereospecific orientations within protein-protein complexes. However, a number of studies in solution have made clear that encounter states are an inherent element of protein complexes (1-8), especially in electron transfer (ET), where the interactions are often extremely fast (9). In the encounter complex, the proteins assume multiple other orientations, often in equilibrium with the major stereospecific state. In low-affinity complexes with dissociation constant (K d ) values > 10 μM, the encounter complex can represent a sizeable fraction, and in some cases, a well-defined, stereospecific complex may even be absent (10-15). The presence of encounter states may be a consequence of the chemical nature of proteins. In nonobligate stereospecific complexes, the interface represents a small fraction of the total protein surface, and therefore, it is reasonable to assume that weak interactions also occur elsewhere. In the case in which protein pairs have evolved to exhibit a high association rate by using electrostatic preorientation, electrostatic patches seem to enhance the presence of encounter states (16,17). On the one hand, the preorientation reduces the surface area that is visited by the partner, thus enhancing the number of productive encounters, but on the other hand, highly charged patches can bind the oppositely charged protein in many orientations with a...

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The Complex of Cytochrome f and Plastocyanin from Nostoc sp. PCC 7119 is Highly Dynamic

Cited by 22 publications

References 31 publications

Kinetic and Structural Characterization of the Interaction between the FMN Binding Domain of Cytochrome P450 Reductase and Cytochrome c

Kinetic and Structural Characterization of the Interaction between the FMN Binding Domain of Cytochrome P450 Reductase and Cytochrome c

Loss of Electrostatic Interactions Causes Increase of Dynamics within the Plastocyanin–Cytochrome f Complex

Identification of productive and futile encounters in an electron transfer protein complex

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