Plastocyanins structure

Fig. 1. Ribbon drawing of the cyanobacterium Synechocystis sp. PCC 6803 Cu(II)-plastocyanin structure showing the secondary structure elements of the protein. The metal ion is represented as a sphere of arbitrary dimensions (Bertini et al., 2001b). The letters N, E, S, and W refer to the cardinal points. The so-called acidic patch present in the structure of plant plastocyanins is located in the E region.

Figure 11 Proposed electron-transfer pathways to the remote and adjacent electron-transfer sites in plastocyanin. Structure from PDB, IPLC...

Structure and electron transfer reactivity of the blue copper protein, plastocyanin. A. G. Sykes, Chem. Soc. Rev., 1985,14, 283 (117). 

Ribbon structures of two redox proteins, cytochrome c (a) and plastocyanin (b). The blowups show the active sites where transition metal atoms are located. 

In the blue, Type I copper proteins plastocyanin and azurin, the active-site structure comprises the trigonal array [CuN2S] of two histidine ligands and one cysteine ligand about the copper,... 

Copper proteins present interesting problems of structure for the copper(I) oxidation state. They are difficult to probe in detail, and what we do know of them suggests they are rarely regular or predictable.58 In plastocyanin the copper(I) coordination sphere is made up of three strongly... 

Bai, Y W., Chung, J., Dyson, H. J., and Wright, P. E. (2001). Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under nondenaturing conditions. Protein Sci. 10, 1056-1066. 

The electrons subsequently pass to plastocyanin (PC), which is a copper-containing protein. The Cu-containing redox center of this 10.5 kD monomer cycles between Cu(I) and Cu(II) oxidation states. The structure of PC shows that... 

Metalloproteins fall into three main structure categories depending on whether the active site consists of a single coordinated metal atom, a metal-porphyrin unit, or metal atoms in a cluster arrangement. In the context of electron-transfer metalloproteins, the blue Cu proteins, cytochromes, and ferre-doxins respectively are examples of these different structure types. Attention will be confined here mainly to a discussion of the reactivity of the blue Cu protein plastocyanin. Reactions of cytochrome c are also considered, with brief mention of the [2Fe-2S] ferredoxin, and high potential Fe/S protein [HIPIP]. 

It is timely to review the reactivity of plastocyanin in the light of recent aqueous solution studies, and the elegant structural work of Freeman and colleagues on both the PCu(I) and PCu(II) forms (1 2) Plastocyanin now ranks alongside cytochrome c (3) as the electron-transfer metalloprotein for which there is most structural information. 

From 13 completed amino-acid sequences and 54 partial sequences (>40 residues) of plastocyanins from higher plants it appears that sixty residues are invariant and 7 are conservatively substituted 02,7). With three algal plastocyanins included there are 39 invariant or conservatively substituted groups. It is believed that the same structural features apply to the whole family, and that highly conserved residues are an indication of functional sites on the protein surface. The upper hydrophobic and right-hand-side surfaces are believed to be particularly relevant in this context, the latter including four consecutive... 

Figure 1. Structure of plastocyanin (2) showing the positions of a-carbon atoms of amino acid residues. The active site and positions of the conserved (plant) negative patch (42-45) and Tyr 83 are indicated (%).

Curiously, solution structures of azurin studied by NMR are not listed in the protein data bank as of 2001, although many NMR structures of plastocyanin are available as will be discussed below. 

A solution structure of French Bean plastocyanin has been reported by Wright and co-workers,19 using nuclear magnetic resonance techniques described in Section 3.5 of Chapter 3. The structure, determined from a plastocyanin molecule in solution rather than in a solid-state crystal, agrees well with that of reduced poplar plastocyanin X-ray crystallographic structure reported above. Conformations of protein side chains constituting the hydrophobic core of the French bean plastocyanin are well-defined by the NMR technique. Surface side chains show... 

This discussion of copper-containing enzymes has focused on structure and function information for Type I blue copper proteins azurin and plastocyanin, Type III hemocyanin, and Type II superoxide dismutase s structure and mechanism of activity. Information on spectral properties for some metalloproteins and their model compounds has been included in Tables 5.2, 5.3, and 5.7. One model system for Type I copper proteins39 and one for Type II centers40 have been discussed. Many others can be found in the literature. A more complete discussion, including mechanistic detail, about hemocyanin and tyrosinase model systems has been included. Models for the blue copper oxidases laccase and ascorbate oxidases have not been discussed. Students are referred to the references listed in the reference section for discussion of some other model systems. Many more are to be found in literature searches.50... 

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