Electron transfer by domain movement in cytochrome bc1
The cytochrome bc 1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc 1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray cryst...
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| Veröffentlicht in: | Nature (London) 1998-04, Vol.392 (6677), p.677-684 |
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| container_volume | 392 |
| creator | Zhang, Zhaolei Huang, Lishar Shulmeister, Vladimir M. Chi, Young-In Kim, Kyeong Kyu Hung, Li-Wei Crofts, Antony R. Berry, Edward A. Kim, Sung-Hou |
| description | The cytochrome
bc
1
is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome
bc
1
transfers electrons from ubiquinol to cytochrome
c
and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe–S protein by ubiquinol. The other site is close enough to cytochrome
c
1
to allow oxidation of the Fe–S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe–S component in order to shuttle electrons from ubiquinol to cytochrome
c
1
. Such a mechanism has not previously been observed in redox protein complexes. |
| doi_str_mv | 10.1038/33612 |
| format | Article |
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bc
1
is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome
bc
1
transfers electrons from ubiquinol to cytochrome
c
and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe–S protein by ubiquinol. The other site is close enough to cytochrome
c
1
to allow oxidation of the Fe–S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe–S component in order to shuttle electrons from ubiquinol to cytochrome
c
1
. Such a mechanism has not previously been observed in redox protein complexes.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/33612</identifier><identifier>PMID: 9565029</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Antimycin A - analogs & derivatives ; Antimycin A - metabolism ; Binding Sites ; Biological and medical sciences ; Cattle ; Chemical reactions ; Chickens ; Crystallography ; Crystallography, X-Ray ; Cytochrome ; Cytochrome c Group - chemistry ; Electrochemistry ; Electron Transport ; Electron Transport Complex III - chemistry ; Electrons ; Enzymes ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; Humans ; Iron-Sulfur Proteins - chemistry ; Membranes ; Metabolism ; Methacrylates ; Models, Chemical ; Models, Molecular ; multidisciplinary ; Oxidation ; Oxidation-Reduction ; Oxidoreductases ; Polyenes - metabolism ; Protein Conformation ; Rabbits ; Respiratory system ; Science ; Science (multidisciplinary) ; Thiazoles - metabolism</subject><ispartof>Nature (London), 1998-04, Vol.392 (6677), p.677-684</ispartof><rights>Macmillan Magazines Ltd. 1998</rights><rights>1998 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Apr 16, 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3722-d5e23a2ff2608902b201a2ca5b223f2d643d6933a84c1d435a7cf2f2212af4213</citedby><cites>FETCH-LOGICAL-c3722-d5e23a2ff2608902b201a2ca5b223f2d643d6933a84c1d435a7cf2f2212af4213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/33612$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/33612$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2187811$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9565029$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Zhaolei</creatorcontrib><creatorcontrib>Huang, Lishar</creatorcontrib><creatorcontrib>Shulmeister, Vladimir M.</creatorcontrib><creatorcontrib>Chi, Young-In</creatorcontrib><creatorcontrib>Kim, Kyeong Kyu</creatorcontrib><creatorcontrib>Hung, Li-Wei</creatorcontrib><creatorcontrib>Crofts, Antony R.</creatorcontrib><creatorcontrib>Berry, Edward A.</creatorcontrib><creatorcontrib>Kim, Sung-Hou</creatorcontrib><title>Electron transfer by domain movement in cytochrome bc1</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>The cytochrome
bc
1
is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome
bc
1
transfers electrons from ubiquinol to cytochrome
c
and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe–S protein by ubiquinol. The other site is close enough to cytochrome
c
1
to allow oxidation of the Fe–S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe–S component in order to shuttle electrons from ubiquinol to cytochrome
c
1
. Such a mechanism has not previously been observed in redox protein complexes.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antimycin A - analogs & derivatives</subject><subject>Antimycin A - metabolism</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Chemical reactions</subject><subject>Chickens</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Cytochrome</subject><subject>Cytochrome c Group - chemistry</subject><subject>Electrochemistry</subject><subject>Electron Transport</subject><subject>Electron Transport Complex III - chemistry</subject><subject>Electrons</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>Membranes</subject><subject>Metabolism</subject><subject>Methacrylates</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>multidisciplinary</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases</subject><subject>Polyenes - metabolism</subject><subject>Protein Conformation</subject><subject>Rabbits</subject><subject>Respiratory system</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Thiazoles - metabolism</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp90FtLwzAYBuAgypxzP0Eo4uGqmnxJ0-RSxjzAwBu9LmmaaEfbzKQT9u-NrszDhVcJvA9f8r0ITQm-IpiKa0o5gT00JiznKeMi30djjEGkWFB-iI5CWGKMM5KzERrJjGcY5BjxeWN0712X9F51wRqflJukcq2qu6R176Y1XZ_Eu970Tr9615qk1OQYHVjVBDMdzgl6vp0_ze7TxePdw-xmkWqaA6RVZoAqsBY4FhJDCZgo0CorAaiFijNacUmpEkyTitFM5dqCBSCgLANCJ-hiO3fl3dvahL5o66BN06jOuHUocimI5JJFePk_ZJQLKWke5ekfuXRr38UtCsCMCcIwjeh8i7R3IXhji5WvW-U3BcHFZ93FV93RnQzD1mVrqp0a-o352ZCroFVjY8e6DjsGROSC_FgzxKR7Mf77T7_f-wB3Uo8Z</recordid><startdate>19980416</startdate><enddate>19980416</enddate><creator>Zhang, Zhaolei</creator><creator>Huang, Lishar</creator><creator>Shulmeister, Vladimir M.</creator><creator>Chi, Young-In</creator><creator>Kim, Kyeong Kyu</creator><creator>Hung, Li-Wei</creator><creator>Crofts, Antony R.</creator><creator>Berry, Edward A.</creator><creator>Kim, Sung-Hou</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</general><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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>7X8</scope></search><sort><creationdate>19980416</creationdate><title>Electron transfer by domain movement in cytochrome bc1</title><author>Zhang, Zhaolei ; Huang, Lishar ; Shulmeister, Vladimir M. ; Chi, Young-In ; Kim, Kyeong Kyu ; Hung, Li-Wei ; Crofts, Antony R. ; Berry, Edward A. ; Kim, Sung-Hou</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3722-d5e23a2ff2608902b201a2ca5b223f2d643d6933a84c1d435a7cf2f2212af4213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antimycin A - analogs & derivatives</topic><topic>Antimycin A - metabolism</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Chemical reactions</topic><topic>Chickens</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>Cytochrome</topic><topic>Cytochrome c Group - chemistry</topic><topic>Electrochemistry</topic><topic>Electron Transport</topic><topic>Electron Transport Complex III - chemistry</topic><topic>Electrons</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Iron-Sulfur Proteins - chemistry</topic><topic>Membranes</topic><topic>Metabolism</topic><topic>Methacrylates</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>multidisciplinary</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases</topic><topic>Polyenes - metabolism</topic><topic>Protein Conformation</topic><topic>Rabbits</topic><topic>Respiratory system</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Thiazoles - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Zhaolei</creatorcontrib><creatorcontrib>Huang, Lishar</creatorcontrib><creatorcontrib>Shulmeister, Vladimir M.</creatorcontrib><creatorcontrib>Chi, Young-In</creatorcontrib><creatorcontrib>Kim, Kyeong Kyu</creatorcontrib><creatorcontrib>Hung, Li-Wei</creatorcontrib><creatorcontrib>Crofts, Antony R.</creatorcontrib><creatorcontrib>Berry, Edward A.</creatorcontrib><creatorcontrib>Kim, Sung-Hou</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Zhaolei</au><au>Huang, Lishar</au><au>Shulmeister, Vladimir M.</au><au>Chi, Young-In</au><au>Kim, Kyeong Kyu</au><au>Hung, Li-Wei</au><au>Crofts, Antony R.</au><au>Berry, Edward A.</au><au>Kim, Sung-Hou</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electron transfer by domain movement in cytochrome bc1</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1998-04-16</date><risdate>1998</risdate><volume>392</volume><issue>6677</issue><spage>677</spage><epage>684</epage><pages>677-684</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>The cytochrome
bc
1
is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome
bc
1
transfers electrons from ubiquinol to cytochrome
c
and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe–S protein by ubiquinol. The other site is close enough to cytochrome
c
1
to allow oxidation of the Fe–S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe–S component in order to shuttle electrons from ubiquinol to cytochrome
c
1
. Such a mechanism has not previously been observed in redox protein complexes.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>9565029</pmid><doi>10.1038/33612</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1998-04, Vol.392 (6677), p.677-684 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79819694 |
| source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | Analytical, structural and metabolic biochemistry Animals Antimycin A - analogs & derivatives Antimycin A - metabolism Binding Sites Biological and medical sciences Cattle Chemical reactions Chickens Crystallography Crystallography, X-Ray Cytochrome Cytochrome c Group - chemistry Electrochemistry Electron Transport Electron Transport Complex III - chemistry Electrons Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Humans Iron-Sulfur Proteins - chemistry Membranes Metabolism Methacrylates Models, Chemical Models, Molecular multidisciplinary Oxidation Oxidation-Reduction Oxidoreductases Polyenes - metabolism Protein Conformation Rabbits Respiratory system Science Science (multidisciplinary) Thiazoles - metabolism |
| title | Electron transfer by domain movement in cytochrome bc1 |
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