Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme
Previous work from this laboratory has revealed a complex and interactive redox behavior for the active metal centers in beef heart cytochrome aa3. All of these centers are contained in two of the 13 subunits which make up the enzyme. The isolated cytochrome aa3 of Paracoccus denitrificans contains...
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| Veröffentlicht in: | Biophysical journal 1991-08, Vol.60 (2), p.408-414 |
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| creator | Pardhasaradhi, K. Ludwig, B. Hendler, R.W. |
| description | Previous work from this laboratory has revealed a complex and interactive redox behavior for the active metal centers in beef heart cytochrome aa3. All of these centers are contained in two of the 13 subunits which make up the enzyme. The isolated cytochrome aa3 of Paracoccus denitrificans contains only two subunits. The purpose of the current investigation was to see if the complex redox behavior is dependent on the presence of the additional 11 peptides that are present in the mammalian enzyme. In this paper we report that the structurally simpler bacterial enzyme displays a redox behavior which is very similar to that seen with the mammalian enzyme. Therefore, the observed redox behavior does not depend on interactions involving the additional peptides. |
| doi_str_mv | 10.1016/S0006-3495(91)82066-5 |
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Psychology</subject><subject>Molecular biophysics</subject><subject>Myocardium - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Paracoccus denitrificans - enzymology</subject><subject>Potentiometry</subject><subject>Protein Conformation</subject><subject>Species Specificity</subject><subject>Spectrophotometry</subject><subject>Terminology as Topic</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9rFDEUxQdR6lr9CIU8iOjD1NzMJDvzYpHFf1CwoD6HO8mNG9mZrEmmZf0ifl3T7rLVJ58SOL97cnNOVZ0BPwcO6vUXzrmqm7aXL3t41QmuVC0fVAuQrag579TDanFEHldPUvrBOQjJ4aQ6ASUl78Si-n0VMk3Zh5Fy9IbhZFnakskRNyzl2XpK7MbnNctrYvkm1Gke5slnZnY5mHUsgwyxYa7c2BVGNMGYOTFLBYreeYNTOmerMG4x-hSmezdojmYDkWNrwpgZTb92Iz2tHjncJHp2OE-rb-_ffV19rC8_f_i0entZm5YrWQvi0LYd8rbp0IqmaZxth6FVxg5OOGFbCUU1MKgB2qWTTiEf0JZcOtv02JxWb_a-23kYyZqSRfm53kY_YtzpgF7_q0x-rb-Haw1Ccb5cFoMXB4MYfs6Ush59MrTZ4ERhTnopAKQSUEC5B00MKUVyx0eA69tG9V2j-rYu3YO-a1TLMnf294b3U_sKi_78oGMyuHERJ-PTEZOiA-j7gl3sMSppXnuKOhlPkyHrY6lb2-D_s8gfzcrBmg</recordid><startdate>19910801</startdate><enddate>19910801</enddate><creator>Pardhasaradhi, K.</creator><creator>Ludwig, B.</creator><creator>Hendler, R.W.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19910801</creationdate><title>Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. 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Psychology</topic><topic>Molecular biophysics</topic><topic>Myocardium - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Paracoccus denitrificans - enzymology</topic><topic>Potentiometry</topic><topic>Protein Conformation</topic><topic>Species Specificity</topic><topic>Spectrophotometry</topic><topic>Terminology as Topic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pardhasaradhi, K.</creatorcontrib><creatorcontrib>Ludwig, B.</creatorcontrib><creatorcontrib>Hendler, R.W.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pardhasaradhi, K.</au><au>Ludwig, B.</au><au>Hendler, R.W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1991-08-01</date><risdate>1991</risdate><volume>60</volume><issue>2</issue><spage>408</spage><epage>414</epage><pages>408-414</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>Previous work from this laboratory has revealed a complex and interactive redox behavior for the active metal centers in beef heart cytochrome aa3. All of these centers are contained in two of the 13 subunits which make up the enzyme. The isolated cytochrome aa3 of Paracoccus denitrificans contains only two subunits. The purpose of the current investigation was to see if the complex redox behavior is dependent on the presence of the additional 11 peptides that are present in the mammalian enzyme. In this paper we report that the structurally simpler bacterial enzyme displays a redox behavior which is very similar to that seen with the mammalian enzyme. Therefore, the observed redox behavior does not depend on interactions involving the additional peptides.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>1655082</pmid><doi>10.1016/S0006-3495(91)82066-5</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 1991-08, Vol.60 (2), p.408-414 |
| issn | 0006-3495 1542-0086 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Animals Biological and medical sciences Cattle Electron Transport Complex IV - chemistry Electron Transport Complex IV - metabolism Fundamental and applied biological sciences. Psychology Molecular biophysics Myocardium - enzymology Oxidation-Reduction Paracoccus denitrificans - enzymology Potentiometry Protein Conformation Species Specificity Spectrophotometry Terminology as Topic |
| title | Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme |
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