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    <title>UTas ePrints - An electrospray mass spectrometric and voltammetric study of horse heart cytochrome c in the presence of metal ions</title>
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    <meta content="Bond, A.M." name="eprints.creators_name" />
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<meta content="Studies on cytochrome c in the presence of a range of biologically essential (Ca2+, Mg2+, Zn2+, Ni2+ and Co2+ ) and toxic ( MeHg+, Cd2+ and Pb2+) metal ions have been undertaken by both cyclic voltammetry at a 4,4'-bipyridyi disulfide modified gold electrode and by electrospray mass spectrometry. Some bases for comparison of data obtained by the two techniques were achieved by compromising solvent
systems and electrolyte (buffer) concentrations with which these techniques are commonly used. The most compatible solvent/electrolyte system for these techniques was found to be 65:35 water:isopropanol with acetic acid, and/or ammonium acetate being added to provide acid, electrolyte and buffer. The electrospray mass spectra of cytochrome c obtained at increased acid concentrations showed a shift in the spectral prolile to lower mass-to-charge ratios, indicating an increase in the charge density of cytochrome c. The additiion of metal salts to the electrospray solution produced metal ion adduction, the number of metal ions binding to the protein increasing with metal salt concentration. Howevcr, the adduc|ion of metal ions to cytochrome c did not alter the overall charge of the protein. Electrospray mass spectrometry and cyclic voltammetry showed that the heme group was neither lost nor replaced by any of the added metal ions, Voltammetric measurements indicate that no preferential binding of metal ions to either the Fe(Ill) or Fe(II) oxidation states ccurs, since the reversible potential obtained
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systems and electrolyte (buffer) concentrations with which these techniques are commonly used. The most compatible solvent/electrolyte system for these techniques was found to be 65:35 water:isopropanol with acetic acid, and/or ammonium acetate being added to provide acid, electrolyte and buffer. The electrospray mass spectra of cytochrome c obtained at increased acid concentrations showed a shift in the spectral prolile to lower mass-to-charge ratios, indicating an increase in the charge density of cytochrome c. The additiion of metal salts to the electrospray solution produced metal ion adduction, the number of metal ions binding to the protein increasing with metal salt concentration. Howevcr, the adduc|ion of metal ions to cytochrome c did not alter the overall charge of the protein. Electrospray mass spectrometry and cyclic voltammetry showed that the heme group was neither lost nor replaced by any of the added metal ions, Voltammetric measurements indicate that no preferential binding of metal ions to either the Fe(Ill) or Fe(II) oxidation states ccurs, since the reversible potential obtained
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    <h1 class="ep_tm_pagetitle">An electrospray mass spectrometric and voltammetric study of horse heart cytochrome c in the presence of metal ions</h1>
    <p style="margin-bottom: 1em" class="not_ep_block"><span class="person_name">Bond, A.M.</span> and <span class="person_name">Colton, R.</span> and <span class="person_name">D'Agostino, A.</span> and <span class="person_name">Traeger, J.C.</span> and <span class="person_name">Downard, A.J.</span> and <span class="person_name">Canty, A.J.</span> (1998) <xhtml:em>An electrospray mass spectrometric and voltammetric study of horse heart cytochrome c in the presence of metal ions.</xhtml:em> Inorganica Chimica Acta, 267 (2). pp. 281-291. ISSN 0020-1693</p><p style="margin-bottom: 1em" class="not_ep_block"></p><table style="margin-bottom: 1em" class="not_ep_block"><tr><td valign="top" style="text-align:center"><a href="http://eprints.utas.edu.au/2881/1/ICA1998_2C_281.pdf"><img alt="[img]" src="http://eprints.utas.edu.au/style/images/fileicons/application_pdf.png" border="0" class="ep_doc_icon" /></a></td><td valign="top"><a href="http://eprints.utas.edu.au/2881/1/ICA1998_2C_281.pdf"><span class="ep_document_citation">PDF</span></a> - Full text restricted - Requires a PDF viewer<br />1881Kb</td><td><form method="get" accept-charset="utf-8" action="http://eprints.utas.edu.au/cgi/request_doc"><input value="4117" name="docid" accept-charset="utf-8" type="hidden" /><div class=""><input value="Request a copy" name="_action_null" class="ep_form_action_button" onclick="return EPJS_button_pushed( '_action_null' )" type="submit" /> </div></form></td></tr></table><p style="margin-bottom: 1em" class="not_ep_block">Official URL: <a href="http://dx.doi.org/10.1016/S0020-1693(97)05775-7">http://dx.doi.org/10.1016/S0020-1693(97)05775-7</a></p><div class="not_ep_block"><h2>Abstract</h2><p style="padding-bottom: 16px; text-align: left; margin: 1em auto 0em auto">Studies on cytochrome c in the presence of a range of biologically essential (Ca2+, Mg2+, Zn2+, Ni2+ and Co2+ ) and toxic ( MeHg+, Cd2+ and Pb2+) metal ions have been undertaken by both cyclic voltammetry at a 4,4'-bipyridyi disulfide modified gold electrode and by electrospray mass spectrometry. Some bases for comparison of data obtained by the two techniques were achieved by compromising solvent&#13;
systems and electrolyte (buffer) concentrations with which these techniques are commonly used. The most compatible solvent/electrolyte system for these techniques was found to be 65:35 water:isopropanol with acetic acid, and/or ammonium acetate being added to provide acid, electrolyte and buffer. The electrospray mass spectra of cytochrome c obtained at increased acid concentrations showed a shift in the spectral prolile to lower mass-to-charge ratios, indicating an increase in the charge density of cytochrome c. The additiion of metal salts to the electrospray solution produced metal ion adduction, the number of metal ions binding to the protein increasing with metal salt concentration. Howevcr, the adduc|ion of metal ions to cytochrome c did not alter the overall charge of the protein. Electrospray mass spectrometry and cyclic voltammetry showed that the heme group was neither lost nor replaced by any of the added metal ions, Voltammetric measurements indicate that no preferential binding of metal ions to either the Fe(Ill) or Fe(II) oxidation states ccurs, since the reversible potential obtained&#13;
from voltammetric measurements did not change following tile metal salt additions.</p></div><table style="margin-bottom: 1em" border="0" cellpadding="3" class="not_ep_block"><tr><th valign="top" class="ep_row">Item Type:</th><td valign="top" class="ep_row">Article</td></tr><tr><th valign="top" class="ep_row">Additional Information:</th><td valign="top" class="ep_row">The definitive version is available at http://www.sciencedirect.com&#13;
</td></tr><tr><th valign="top" class="ep_row">Subjects:</th><td valign="top" class="ep_row"><a href="http://eprints.utas.edu.au/view/subjects/250204.html">250000 Chemical Sciences &gt; 250200 Inorganic Chemistry &gt; 250204 Bioinorganic Chemistry</a></td></tr><tr><th valign="top" class="ep_row">ID Code:</th><td valign="top" class="ep_row">2881</td></tr><tr><th valign="top" class="ep_row">Deposited By:</th><td valign="top" class="ep_row"><span class="ep_name_citation"><span class="person_name">Prof Allan J Canty</span></span></td></tr><tr><th valign="top" class="ep_row">Deposited On:</th><td valign="top" class="ep_row">16 Jan 2008 11:01</td></tr><tr><th valign="top" class="ep_row">Last Modified:</th><td valign="top" class="ep_row">16 Jan 2008 11:01</td></tr><tr><th valign="top" class="ep_row">ePrint Statistics:</th><td valign="top" class="ep_row"><a target="ePrintStats" href="/es/index.php?action=show_detail_eprint;id=2881;">View statistics for this ePrint</a></td></tr></table><p align="right">Repository Staff Only: <a href="http://eprints.utas.edu.au/cgi/users/home?screen=EPrint::View&amp;eprintid=2881">item control page</a></p>
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