The Ternary Complex of Cytochrome f and Cytochrome c: Identification of a Second Binding Site and Competition for Plastocyanin Binding

Crowley, Peter B.; Rabe, Kersten S.; Worrall, J.A.R.; Canters, Gerard W.; Ubbink, Marcellus

doi:10.1002/1439-7633(20020603)3:6<526::aid-cbic526>3.0.co;2-n

Cited by 36 publications

(42 citation statements)

References 29 publications

(43 reference statements)

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“…Interestingly, in a quite recent study, two binding site for cytochrome c were identified on cytochrome f, involved in formation of a non-physiological complex [25].…”

Section: Nmr Experimentsmentioning

confidence: 99%

“…In this respect, it is also worth noting that the interface regions on cytochrome c in the Salemme model and in the electrostatically dominant model are adjacent. The importance of inter-protein dynamics in electron transfer complexes appears to be quite different in different systems [14,24,25], but likely plays a crucial role in modulating the rate of the process [68].…”

Section: Comparison With Previous Studiesmentioning

confidence: 99%

“…In a similar approach, heteronuclear NMR and docking calculations were used for building structural models of the cytochrome c 553 -ferredoxin complex and a combination of TROSY experiments and docking calculations were used for the study of the [Fe]-hydrogenase-cytochrome c 553 complex [22,23]. Other, more recent, applications of similar strategies include the cytochrome b 5 -myoglobin [24] and the cytochrome ccytochrome f [25] complexes. The present approach can thus be seen as a general strategy for the investigation of adducts between electron transfer proteins.…”

Section: Introductionmentioning

confidence: 99%

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A further investigation of the cytochrome b 5–cytochrome c complex

et al. 2003

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The interaction of reduced rabbit cytochrome b 5 with reduced yeast iso-1 cytochrome c has been studied through the analysis of 1 H-15 N HSQC spectra, of 15 N longitudinal (R 1 ) and transverse (R 2 ) relaxation rates, and of the solvent exchange rates of protein backbone amides. For the first time, the adduct has been investigated also from the cytochrome c side. The analysis of the NMR data was integrated with docking calculations. The result is that cytochrome b 5 has two negative patches capable of interacting with a single positive surface area of cytochrome c. At low protein concentrations and in equimolar mixture, two different 1:1 adducts are formed. At high concentration and/or with excess cytochrome c, a 2:1 adduct is formed. All the species are in fast exchange on the scale of differences in chemical shift. By comparison with literature data, it appears that the structure of one 1:1 adduct changes with the origin or primary sequence of cytochrome b 5 .

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“…Interestingly, in a quite recent study, two binding site for cytochrome c were identified on cytochrome f, involved in formation of a non-physiological complex [25].…”

Section: Nmr Experimentsmentioning

confidence: 99%

Section: Comparison With Previous Studiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A further investigation of the cytochrome b 5–cytochrome c complex

et al. 2003

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“…4B). It can be concluded that the binding affinity of cytf for Ana-cytc 6 is ϳ10 4 M Ϫ1 , which is about 2 orders of magnitude greater than the affinity for the physiological partner, P. laminosum Pc (15,29). From the ratio of the observed ⌬␦ Bind to the fitted ⌬␦ Max (Fig.…”

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confidence: 96%

“…The different roles of electrostatics and hydrophobics can be further illustrated by comparison with the recently characterized, non-physiological complex of yeast cytochrome c (cytc) and cytf (29). It was found that cytf binds two equivalents of cytc with binding constants of ϳ2 ϫ 10 4 M Ϫ1 and 4 ϫ 10 3 M Ϫ1 .…”

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confidence: 99%

The Interactions of Cyanobacterial Cytochromec6 and Cytochrome f, Characterized by NMR

Crowley¹,

Díaz‐Quintana²,

Molina-Heredia³

et al. 2002

Journal of Biological Chemistry

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Protein Recognition

Mansfield

Cross

Matthews

et al. 2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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Proteins function by making and breaking interactions with other molecules. The identities of these molecules cover the full spectrum of substances that one might find in an organism, illustrating the astounding structural and functional diversity that can be obtained from different combinations of roughly 20 amino acids. Thus, proteins are able to form functional interactions with partners ranging from metal ions and small diatomic molecules, such as oxygen and nitric oxide, through to typical organic molecules and macromolecules, such as nucleic acid polymers, polysaccharides, and of course other proteins. Given the enormous breadth of these interactions and the functions that they bring about, we have chosen in this chapter to focus on capturing a few of the general principles underlying protein recognition. As other chapters in this volume deal in depth with enzymes and enzyme-substrate interactions, we focus here on protein-protein and protein-DNA recognition.First, we discuss the general physicochemical nature of the interfaces made between proteins and their partners, the strength of these interactions, and methods for measuring their strength. Next, we describe two areas of protein recognition that have recently received much attention: coupled folding and binding, in which at least one of the partners in a protein interaction is disordered in the absence of its partner, and the regulation of protein interactions by post-translational modification (PTM) -a phenomenon that underlies diverse biological processes such as signaling and gene regulation. Finally, we look at progress that has been made in exploiting our understanding of protein recognition to either inhibit protein-protein interactions or to engineer new interactions for research or therapeutic purposes.

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The Ternary Complex of Cytochrome f and Cytochrome c: Identification of a Second Binding Site and Competition for Plastocyanin Binding

Cited by 36 publications

References 29 publications

A further investigation of the cytochrome b 5–cytochrome c complex

A further investigation of the cytochrome b 5–cytochrome c complex

The Interactions of Cyanobacterial Cytochromec6 and Cytochrome f, Characterized by NMR

Protein Recognition

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