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class="vector-toc-numb">2</span> <span>Blue copper proteins</span> </div> </a> <button aria-controls="toc-Blue_copper_proteins-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Blue copper proteins subsection</span> </button> <ul id="toc-Blue_copper_proteins-sublist" class="vector-toc-list"> <li id="toc-Structure_of_the_Blue_Copper_Proteins_Type_I_Copper_Centers" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Structure_of_the_Blue_Copper_Proteins_Type_I_Copper_Centers"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>Structure of the Blue Copper Proteins Type I Copper Centers</span> </div> </a> <ul id="toc-Structure_of_the_Blue_Copper_Proteins_Type_I_Copper_Centers-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Electronic_structure_of_the_blue_copper_protein_type_I_copper_complexes" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Electronic_structure_of_the_blue_copper_protein_type_I_copper_complexes"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>Electronic structure of the blue copper protein type I copper complexes</span> </div> </a> <ul id="toc-Electronic_structure_of_the_blue_copper_protein_type_I_copper_complexes-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Spectral_changes_with_temperature" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Spectral_changes_with_temperature"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Spectral changes with temperature</span> </div> </a> <ul id="toc-Spectral_changes_with_temperature-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Inner_and_outer_sphere_metal_coordination" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Inner_and_outer_sphere_metal_coordination"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.4</span> <span>Inner and outer sphere metal coordination</span> </div> </a> <ul id="toc-Inner_and_outer_sphere_metal_coordination-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Blue_Copper_Protein_"Entatic_State"" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Blue_Copper_Protein_"Entatic_State""> <div class="vector-toc-text"> <span class="vector-toc-numb">2.5</span> <span>Blue Copper Protein "Entatic State"</span> </div> </a> <ul id="toc-Blue_Copper_Protein_"Entatic_State"-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" 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id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"><span class="mw-redirectedfrom">(Redirected from <a href="/w/index.php?title=Copper_proteins&redirect=no" class="mw-redirect" title="Copper proteins">Copper proteins</a>)</span></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Proteins that contain one or more copper ions as prosthetic groups</div> <p><b>Copper proteins</b> are <a href="/wiki/Proteins" class="mw-redirect" title="Proteins">proteins</a> that contain one or more <a href="/wiki/Copper" title="Copper">copper</a> ions as <a href="/wiki/Prosthetic_group" title="Prosthetic group">prosthetic groups</a>. Copper proteins are found in all forms of air-breathing life. These proteins are usually associated with <a href="/wiki/Electron-transfer" class="mw-redirect" title="Electron-transfer">electron-transfer</a> with or without the involvement of <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> (O<sub>2</sub>). Some organisms even use copper proteins to carry oxygen instead of iron proteins. A prominent copper protein in humans is in <a href="/wiki/Cytochrome_c_oxidase" title="Cytochrome c oxidase">cytochrome c oxidase</a> (cco). This enzyme cco mediates the controlled combustion that produces <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> Other copper proteins include some <a href="/wiki/Superoxide_dismutase" title="Superoxide dismutase">superoxide dismutases</a> used in defense against free radicals, peptidyl-α-monooxygenase for the production of hormones, and tyrosinase, which affects skin pigmentation.<sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Classes">Classes</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=1" title="Edit section: Classes"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The metal centers in the copper proteins can be classified into several types:<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> </p> <ul><li><b>Type I copper centres (T1Cu)</b> are characterized by a single copper atom coordinated by two <a href="/wiki/Histidine" title="Histidine">histidine</a> residues and a <a href="/wiki/Cysteine" title="Cysteine">cysteine</a> residue in a <a href="/wiki/Trigonal_planar" class="mw-redirect" title="Trigonal planar">trigonal planar</a> structure, and a variable axial <a href="/wiki/Ligand" title="Ligand">ligand</a>. In <a href="/wiki/Plastocyanin_family_of_copper_binding_proteins" class="mw-redirect" title="Plastocyanin family of copper binding proteins">class I T1Cu proteins</a> (e.g. <a href="/wiki/Amicyanin" title="Amicyanin">amicyanin</a>, <a href="/wiki/Plastocyanin" title="Plastocyanin">plastocyanin</a> and pseudoazurin) the axial ligand is the sulfur of <a href="/wiki/Methionine" title="Methionine">methionine</a>, whereas aminoacids other than methionine (e.g. <a href="/wiki/Glutamine" title="Glutamine">glutamine</a>) give rise to class II T1Cu copper proteins. <a href="/wiki/Azurin" title="Azurin">Azurins</a> contain the third type of T1Cu centres: besides a methionine in one axial position, they contain a second axial ligand (a <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl group</a> of a <a href="/wiki/Glycine" title="Glycine">glycine</a> residue). T1Cu-containing proteins are usually called "cupredoxins", and show similar three-dimensional structures, relatively high reduction potentials (> 250 mV), and strong absorption near 600 nm (due to <a href="/wiki/Sulfur" title="Sulfur">S</a>→<a href="/wiki/Copper" title="Copper">Cu</a> <a href="/wiki/Luminophore" title="Luminophore">charge transfer</a>), which usually gives rise to a blue colour. Cupredoxins are therefore often called "blue copper proteins". This may be misleading, since some T1Cu centres also absorb around 460 nm and are therefore green. When studied by <a href="/wiki/Electron_spin_resonance" class="mw-redirect" title="Electron spin resonance">EPR</a> spectroscopy, T1Cu centres show small hyperfine splittings in the parallel region of the spectrum (compared to common copper coordination compounds).<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup></li> <li><b>Type II copper centres (T2Cu)</b> exhibit a <a href="/wiki/Square_planar" class="mw-redirect" title="Square planar">square planar</a> coordination by N or N/O <a href="/wiki/Ligand" title="Ligand">ligands</a>. They exhibit an axial <a href="/wiki/Electron_spin_resonance" class="mw-redirect" title="Electron spin resonance">EPR</a> spectrum with copper <a href="/wiki/Hyperfine_structure" title="Hyperfine structure">hyperfine splitting</a> in the parallel region similar to that observed in regular copper coordination compounds. Since no sulfur ligation is present, the optical spectra of these centres lack distinctive features. T2Cu centres occur in <a href="/wiki/Enzyme" title="Enzyme">enzymes</a>, where they assist in oxidations or oxygenations.<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup></li> <li><b>Type III copper centres (T3Cu)</b> consist of a pair of copper centres, each coordinated by three histidine residues. These proteins exhibit no EPR signal due to strong antiferromagnetic coupling (i.e. spin pairing) between the two S = 1/2 metal ions due to their covalent overlap with a <a href="/wiki/Bridging_ligand" title="Bridging ligand">bridging ligand</a>. These centres are present in some oxidases and <a href="/wiki/Transition_metal_dioxygen_complex" title="Transition metal dioxygen complex">oxygen-transporting proteins</a> (e.g. <a href="/wiki/Hemocyanin" title="Hemocyanin">hemocyanin</a> and <a href="/wiki/Tyrosinase" title="Tyrosinase">tyrosinase</a>).<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup></li> <li>Binuclear <b>Copper A centres (Cu<sub>A</sub>)</b> are found in <a href="/wiki/Cytochrome_c_oxidase" title="Cytochrome c oxidase">cytochrome <i>c</i> oxidase</a> and <a href="/wiki/Nitrous-oxide_reductase" title="Nitrous-oxide reductase">nitrous-oxide reductase</a> (<a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> <a rel="nofollow" class="external text" href="https://enzyme.expasy.org/EC/1.7.99.6">1.7.99.6</a>). The two copper atoms are coordinated by two histidines, one methionine, a protein backbone carbonyl oxygen, and two bridging cysteine residues.<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup></li> <li><b>Copper B centres (Cu<sub>B</sub>)</b> are found in <a href="/wiki/Cytochrome_c_oxidase" title="Cytochrome c oxidase">cytochrome <i>c</i> oxidase</a>. The copper atom is coordinated by three histidines in trigonal pyramidal geometry.</li> <li>A tetranuclear <b>Copper Z centre (Cu<sub>Z</sub>)</b> is found in nitrous-oxide reductase. The four copper atoms are coordinated by seven histidine residues and bridged by a sulfur atom.</li></ul> <div class="mw-heading mw-heading2"><h2 id="Blue_copper_proteins">Blue copper proteins</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=2" title="Edit section: Blue copper proteins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The blue copper proteins owe their name to their intense blue coloration (<a rel="nofollow" class="external text" href="http://www.chemspider.com/Chemical-Structure.25221.html">Cu(II)</a>). The blue copper protein often called as "<a href="/wiki/Protein_moonlighting" title="Protein moonlighting">moonlighting protein</a>", which means a protein can perform more than one function. They serve as electron transfer agents, with the active site shuttling between Cu(I) and Cu(II). The Cu<sup>2+</sup> in the oxidized state can accept one electron to form Cu<sup>1+</sup> in the reduced protein. The geometry of the Cu center has a major impact on its redox properties. The Jahn-Teller distortion does not apply to the blue copper proteins because the copper site has low symmetry that does not support degeneracy in the d-orbital manifold. The absence of large reorganizational changes enhances the rate of their electron transfer. The active site of a type-I blue copper protein. Two 2-histidines, 1 methionine and 1 cysteine present in the coordination sphere. Example for Type-I blue copper protein are <a href="/wiki/Plastocyanin" title="Plastocyanin">plastocyanine</a> , <a href="/wiki/Azurin" title="Azurin">azurin</a>, and nitrite reductase, <a href="/wiki/Hemocyanin" title="Hemocyanin">haemocyanin</a> and <a href="/wiki/Tyrosinase" title="Tyrosinase">tyrosinase</a>. </p> <div class="mw-heading mw-heading3"><h3 id="Structure_of_the_Blue_Copper_Proteins_Type_I_Copper_Centers">Structure of the Blue Copper Proteins Type I Copper Centers</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=3" title="Edit section: Structure of the Blue Copper Proteins Type I Copper Centers"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The Blue Copper Proteins, a class of Type 1 copper proteins, are small proteins containing a cupredoxin fold and a single Type I copper ion coordinated by two <a href="/wiki/Histidine" title="Histidine">histidine</a> N-donors, a <a href="/wiki/Cysteine" title="Cysteine">cysteine</a> thiolate S-donor and a <a href="/wiki/Methionine" title="Methionine">methionine</a> thioether S-donor.<sup id="cite_ref-:0_8-0" class="reference"><a href="#cite_note-:0-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> In the oxidized state, the <a href="/wiki/Cu2%2B" class="mw-redirect" title="Cu2+">Cu<sup>+2</sup></a> ion will form either a trigonal bipyramidal or tetrahedral coordination.<sup id="cite_ref-:0_8-1" class="reference"><a href="#cite_note-:0-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> The Type 1 copper proteins are identified as blue copper proteins due to the <a href="/wiki/Ligand" title="Ligand">ligand</a> to metal charge transfer an intense band at 600 nm that gives the characteristic of a deep blue colour present in the electron absorption spectrum.<sup id="cite_ref-:1_9-0" class="reference"><a href="#cite_note-:1-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Blue_Copper_Protein-_Type_1.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/cc/Blue_Copper_Protein-_Type_1.jpg/397px-Blue_Copper_Protein-_Type_1.jpg" decoding="async" width="397" height="174" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/cc/Blue_Copper_Protein-_Type_1.jpg/596px-Blue_Copper_Protein-_Type_1.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/c/cc/Blue_Copper_Protein-_Type_1.jpg 2x" data-file-width="699" data-file-height="306" /></a><figcaption>The structure of active site of type 1- blue copper protein.</figcaption></figure> <p>The protein structure of a Type 1 blue copper protein, <a href="/wiki/Amicyanin" title="Amicyanin">amicyanin</a>, is built from polypeptide folds that are commonly found in blue copper proteins β sandwich structure.<sup id="cite_ref-:2_10-0" class="reference"><a href="#cite_note-:2-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> The structure is very similar to <a href="/wiki/Plastocyanin" title="Plastocyanin">plastocyanin</a> and <a href="/wiki/Azurin" title="Azurin">azurin</a> as they also identify as Type 1 copper proteins.<sup id="cite_ref-:2_10-1" class="reference"><a href="#cite_note-:2-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> They are also similar to one another due to the geometry of the copper site of each copper protein. The protein azurin has a trigonal bipyramidal geometry with elongated axial glycine and methoinione sulfur ligands. Plastocyanins have an additional methionine sulfur ligand on the axial position. The main difference of each copper protein is that each protein has different number and species of ligand coordinated to the copper center. </p> <div class="mw-heading mw-heading3"><h3 id="Electronic_structure_of_the_blue_copper_protein_type_I_copper_complexes">Electronic structure of the blue copper protein type I copper complexes</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=4" title="Edit section: Electronic structure of the blue copper protein type I copper complexes"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The strong bond between the copper ion and the cysteine sulfur allows for the non-bonded electron on the cysteine sulfur to be present on both the low/high spin state copper ion, d<sub>x</sub><sup>2</sup>-d<sub>y</sub><sup>2</sup> orbital and the <a href="/wiki/P-orbital" class="mw-redirect" title="P-orbital">p-orbital</a> of the cysteine sulfur.<sup id="cite_ref-:1_9-1" class="reference"><a href="#cite_note-:1-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Most copper (II) complexes will exhibit the <a href="/wiki/Jahn%E2%80%93Teller_effect" title="Jahn–Teller effect">Jahn-Teller effect</a> when the complex forms a tetragonal distortion of an <a href="/wiki/Octahedral_molecular_geometry" title="Octahedral molecular geometry">octahedral</a> complex geometry.<sup id="cite_ref-:3_11-0" class="reference"><a href="#cite_note-:3-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> With blue copper proteins, a distorted <a href="/wiki/Tetrahedral_molecular_geometry" title="Tetrahedral molecular geometry">tetrahedral complex</a> will be formed due to the strong equatorial cysteine ligand and the weak axial methionine ligand.<sup id="cite_ref-:3_11-1" class="reference"><a href="#cite_note-:3-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> The two neutral histidine ligands are positioned by the protein ligand so the geometry is distorted tetrahedral. This will cause them not to be able to coordinate perfectly as tetrahedral or a square planar. </p> <div class="mw-heading mw-heading3"><h3 id="Spectral_changes_with_temperature">Spectral changes with temperature</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=5" title="Edit section: Spectral changes with temperature"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Lowering the temperature may change the transitions. The intense absorbance at about 16000 cm<sup>−1</sup> was characterized the absorptions feature of blue copper. There was a second lower energy feature band with moderate absorption intensity. Polarized signal-crystal absorption data on <a href="/wiki/Plastocyanin" title="Plastocyanin">plastocyanin</a> showed that both bands have the same polarization ratio that associated with Cu(II)-S(Cys) bond. This is explained that the normal cupric complex has high energy intense sigma and low energy weak π bonds. However, in the blue copper protein case have low energy intense sigma and high energy weak π bonds because CT intensity reflects overlap of the donor and acceptor orbitals in the CT process. This required that the 3d<sub>(x<sup>2</sup>-y<sup>2</sup> )</sub> orbital of the blue copper site be oriented such that its lobes bisect the <a rel="nofollow" class="external text" href="https://www.researchgate.net/figure/fig1_49837346">Cu-S(Cys)</a> bond giving dominant π overlap with sulfur directly. Finally, the nature of the ground state wave function of the blue copper protein is rich in electron absorption spectrum. </p> <div class="mw-heading mw-heading3"><h3 id="Inner_and_outer_sphere_metal_coordination">Inner and outer sphere metal coordination</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=6" title="Edit section: Inner and outer sphere metal coordination"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The cysteine sulfur copper (II) ion bonds range from 2.6 to 3.2 Å.<sup id="cite_ref-:4_12-0" class="reference"><a href="#cite_note-:4-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> With the reduced form, <a href="/wiki/Copper(I)_iodide" title="Copper(I) iodide">CuI</a>, protein structures are still formed with elongated bonds by 0.1 Å or less. with the oxidized and reduced protein structures, they are superimposable. With <a href="/wiki/Amicyanin" title="Amicyanin">amicyanin</a>, there is an exception due to the histidine being ligated and it is not bound to copper iodide.<sup id="cite_ref-:4_12-1" class="reference"><a href="#cite_note-:4-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> In <a href="/wiki/Azurin" title="Azurin">azurin</a>, the <a href="/wiki/Cysteine" title="Cysteine">Cysteine</a>112 thiolate accepts the hydrogen bonds from the amide backbone of <a href="/wiki/Asparagine" title="Asparagine">Asparagine</a>47, and <a href="/wiki/Phenylalanine" title="Phenylalanine">Phenylalanine</a>114, and <a href="/wiki/Histidine" title="Histidine">Histidine</a>46 donates a hydrogen bond to the carbonyl backbone of Asparagine10. The Cysteine84 <a href="/wiki/Thiol" title="Thiol">thiolate</a> of <a href="/wiki/Plastocyanin" title="Plastocyanin">plastocyanin</a> accepts a hydrogen bond from a amide backbone, <a href="/wiki/Asparagine" title="Asparagine">Asparagine</a>38, and Histidine37 interacts strongly with the carbonyl backbone of <a href="/wiki/Alanine" title="Alanine">Alanine</a>33 and more weakly with the carbonyl backbone of <a href="/wiki/Leucine" title="Leucine">Leucine</a>5, <a href="/wiki/Glycine" title="Glycine">Glycine</a>34, and the amide backbone of Phenylalanine35.<sup id="cite_ref-:4_12-2" class="reference"><a href="#cite_note-:4-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Ligand_Field_Splitting_Diagram_of_Blue_Copper_Protein.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/cb/Ligand_Field_Splitting_Diagram_of_Blue_Copper_Protein.jpg/384px-Ligand_Field_Splitting_Diagram_of_Blue_Copper_Protein.jpg" decoding="async" width="384" height="269" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/c/cb/Ligand_Field_Splitting_Diagram_of_Blue_Copper_Protein.jpg 1.5x" data-file-width="512" data-file-height="359" /></a><figcaption>Ligand field splitting diagram for blue copper protein<sup id="cite_ref-:3_11-2" class="reference"><a href="#cite_note-:3-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup></figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Blue_Copper_Protein_"Entatic_State""><span id="Blue_Copper_Protein_.22Entatic_State.22"></span>Blue Copper Protein "Entatic State"</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=7" title="Edit section: Blue Copper Protein "Entatic State""><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Cu<sup>2+</sup> complexes often have relatively slow transfer rates. An example is the Cu<sup>2+/+</sup> <a href="/wiki/Aquo_complex" class="mw-redirect" title="Aquo complex">aquo complex</a>, which is 5 x 10<sup>−7</sup> M<sup>−1</sup>.sec<sup>−1</sup> compared to the blue copper protein which is between 1ms and 01μs.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> Upon electron transfer the oxidized Cu<sup>2+</sup> state at the blue copper protein active site will be minimized because the Jahn-Teller effect is minimized. The distorted geometry prevents Jahn-Teller distortion. The orbital degeneracy is removed due to the asymmetric ligand field.<sup id="cite_ref-:3_11-3" class="reference"><a href="#cite_note-:3-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> The asymmetric ligand field is influenced by the strong equatorial cysteine ligand and the weak axial methionine ligand. In Figure 2, an energy level diagram shows three different relevant geometries and their d-orbital splitting and the Jahn-Teller effect is shown in blue.<sup id="cite_ref-:3_11-4" class="reference"><a href="#cite_note-:3-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> (i) shows the tetrahedral geometry energy level diagram with a that is degenerate. The tetrahedral structure can undergo Jahn-Teller distortion because of the degenerate orbitals. (ii) shows the C<sub>3v</sub> symmetric geometry energy level splitting diagram with an <sup>2</sup>E ground state that is degenerate. The C<sub>3v</sub> geometry was formed by the elongated methionine thioether bond at the reduced site. The unpaired electrons leads to the Jahn-Teller effect. (iii) shows the ground state energy level splitting diagram of the C<sub>s</sub> geometry with a longer thioester bond and a subsequently shorter thiolate bond. This is the proper geometry of the blue copper protein. This shows that there is no presence of the Jahn-Teller effect. The energy diagram shows that the asymmetry of the short Cu-S(Cys) bond and the highly distorted Cu-L bond angles causes the degeneracy of the orbitals to be removed and thereby removing the Jahn-Teller effect, which is due to the weak donor at an Cu-S(Met) and strong donor at Cu-S(Met).<sup id="cite_ref-:3_11-5" class="reference"><a href="#cite_note-:3-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=8" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Copper_in_health" class="mw-redirect" title="Copper in health">Copper in health</a></li> <li><a href="/wiki/Stellacyanin" title="Stellacyanin">Stellacyanin</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Copper_protein&action=edit&section=9" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist reflist-columns references-column-width" style="column-width: 30em;"> <ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFLontie2018" class="citation book cs1">Lontie R, ed. 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