Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping‐pong kinetic mechanism
The mitochondrial ADP/ATP carrier (SLC25A4), also called the adenine nucleotide translocase, imports ADP into the mitochondrial matrix and exports ATP, which are key steps in oxidative phosphorylation. Historically, the carrier was thought to form a homodimer and to operate by a sequential kinetic m...
Gespeichert in:
| Veröffentlicht in: | EMBO reports 2023-08, Vol.24 (8), p.e57127-n/a |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | n/a |
|---|---|
| container_issue | 8 |
| container_start_page | e57127 |
| container_title | EMBO reports |
| container_volume | 24 |
| creator | Cimadamore‐Werthein, Camila Jaiquel Baron, Stephany King, Martin S Springett, Roger Kunji, Edmund RS |
| description | The mitochondrial ADP/ATP carrier (SLC25A4), also called the adenine nucleotide translocase, imports ADP into the mitochondrial matrix and exports ATP, which are key steps in oxidative phosphorylation. Historically, the carrier was thought to form a homodimer and to operate by a sequential kinetic mechanism, which involves the formation of a ternary complex with the two exchanged substrates bound simultaneously. However, recent structural and functional data have demonstrated that the mitochondrial ADP/ATP carrier works as a monomer and has a single substrate binding site, which cannot be reconciled with a sequential kinetic mechanism. Here, we study the kinetic properties of the human mitochondrial ADP/ATP carrier by using proteoliposomes and transport robotics. We show that the Km/Vmax ratio is constant for all of the measured internal concentrations. Thus, in contrast to earlier claims, we conclude that the carrier operates with a ping‐pong kinetic mechanism in which substrate exchange across the membrane occurs consecutively rather than simultaneously. These data unite the kinetic and structural models, showing that the carrier operates with an alternating access mechanism.
Synopsis
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported.
The kinetics of the mitochondrial ADP/ATP carrier was studied using proteoliposomes and robotic transport assays.
Uptake curves were recorded to provide an accurate assessment of the initial transport rates in different substrate concentration gradients.
In two‐substrate initial‐velocity studies, the ratio of Km/Vmax is constant for all measured internal concentrations of the substrate.
The carrier operates with a ping‐pong kinetic mechanism in which the import and export transport steps occur consecutively.
Graphical Abstract
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported. |
| doi_str_mv | 10.15252/embr.202357127 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10398649</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2845017239</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5147-bf4f20e4fab3e7d4e0e628c54a1e8de7e2192b8eafbe6ff540b44c35f0a03b123</originalsourceid><addsrcrecordid>eNqFkc1uEzEURi0EoqWwZocssWGTxr9jDxuUhpYiBVFBkWBleZw7icuMPdgzrbrjEXhGnoQpCaEgIVa-ks93dK8-hB5Tckglk2wKbZUOGWFcKsrUHbRPRVFOOFX67nZmjH7cQw9yviCEyFLp-2iPK6Y0lXoffTodWhtw6_vo1jEsk7cNnr08m87Oz7CzKXlI-P1izuRM4NhBsj1kfOX7Nba482H1_eu3LoYV_uwD9N7hFtzaBp_bh-hebZsMj7bvAfpwcnw-P50s3r56PZ8tJk5SoSZVLWpGQNS24qCWAggUTDspLAW9BAWMlqzSYOsKirqWglRCOC5rYgmvKOMH6MXG2w1VC0sHoU-2MV3yrU3XJlpv_vwJfm1W8dJQwktdiHI0PNsaUvwyQO5N67ODprEB4pAN04wTwQuqRvTpX-hFHFIY7xspIQlVjN8IpxvKpZhzgnq3DSXmZ2_mpjez621MPLl9xI7_VdQIPN8AV76B6__5zPGbo3e37WQTzmMurCD93vpfC_0Adhi2Cw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2845017239</pqid></control><display><type>article</type><title>Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping‐pong kinetic mechanism</title><source>MEDLINE</source><source>Wiley Journals</source><source>Wiley Online Library Free Content</source><source>Springer Nature OA Free Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Cimadamore‐Werthein, Camila ; Jaiquel Baron, Stephany ; King, Martin S ; Springett, Roger ; Kunji, Edmund RS</creator><creatorcontrib>Cimadamore‐Werthein, Camila ; Jaiquel Baron, Stephany ; King, Martin S ; Springett, Roger ; Kunji, Edmund RS</creatorcontrib><description>The mitochondrial ADP/ATP carrier (SLC25A4), also called the adenine nucleotide translocase, imports ADP into the mitochondrial matrix and exports ATP, which are key steps in oxidative phosphorylation. Historically, the carrier was thought to form a homodimer and to operate by a sequential kinetic mechanism, which involves the formation of a ternary complex with the two exchanged substrates bound simultaneously. However, recent structural and functional data have demonstrated that the mitochondrial ADP/ATP carrier works as a monomer and has a single substrate binding site, which cannot be reconciled with a sequential kinetic mechanism. Here, we study the kinetic properties of the human mitochondrial ADP/ATP carrier by using proteoliposomes and transport robotics. We show that the Km/Vmax ratio is constant for all of the measured internal concentrations. Thus, in contrast to earlier claims, we conclude that the carrier operates with a ping‐pong kinetic mechanism in which substrate exchange across the membrane occurs consecutively rather than simultaneously. These data unite the kinetic and structural models, showing that the carrier operates with an alternating access mechanism.
Synopsis
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported.
The kinetics of the mitochondrial ADP/ATP carrier was studied using proteoliposomes and robotic transport assays.
Uptake curves were recorded to provide an accurate assessment of the initial transport rates in different substrate concentration gradients.
In two‐substrate initial‐velocity studies, the ratio of Km/Vmax is constant for all measured internal concentrations of the substrate.
The carrier operates with a ping‐pong kinetic mechanism in which the import and export transport steps occur consecutively.
Graphical Abstract
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.15252/embr.202357127</identifier><identifier>PMID: 37278158</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adenine ; adenine nucleotide translocator ; Adenine Nucleotide Translocator 1 - metabolism ; Adenosine diphosphate ; Adenosine Diphosphate - metabolism ; Adenosine triphosphate ; Adenosine Triphosphate - metabolism ; ADP/ATP translocase ; ATP ; Binding sites ; Bioenergetics ; Concentration gradient ; Electron transport chain ; EMBO20 ; EMBO21 ; EMBO57 ; Exchanging ; Exports ; Humans ; Imports ; Kinetics ; Life Sciences ; Ligands ; Mitochondria ; Mitochondria - metabolism ; Mitochondrial ADP, ATP Translocases - chemistry ; Mitochondrial ADP, ATP Translocases - metabolism ; mitochondrial carrier family ; Nucleotides ; Oxidative phosphorylation ; Phosphorylation ; Robotics ; SLC25 ; Structural models ; Structure-function relationships ; Substrates ; Translocase</subject><ispartof>EMBO reports, 2023-08, Vol.24 (8), p.e57127-n/a</ispartof><rights>The Author(s) 2023</rights><rights>2023 The Authors. Published under the terms of the CC BY 4.0 license.</rights><rights>2023. This article is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5147-bf4f20e4fab3e7d4e0e628c54a1e8de7e2192b8eafbe6ff540b44c35f0a03b123</citedby><cites>FETCH-LOGICAL-c5147-bf4f20e4fab3e7d4e0e628c54a1e8de7e2192b8eafbe6ff540b44c35f0a03b123</cites><orcidid>0000-0001-6030-5154 ; 0000-0002-0610-4500 ; 0000-0001-5507-817X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10398649/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10398649/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,41120,42189,45574,45575,46409,46833,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37278158$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cimadamore‐Werthein, Camila</creatorcontrib><creatorcontrib>Jaiquel Baron, Stephany</creatorcontrib><creatorcontrib>King, Martin S</creatorcontrib><creatorcontrib>Springett, Roger</creatorcontrib><creatorcontrib>Kunji, Edmund RS</creatorcontrib><title>Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping‐pong kinetic mechanism</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>The mitochondrial ADP/ATP carrier (SLC25A4), also called the adenine nucleotide translocase, imports ADP into the mitochondrial matrix and exports ATP, which are key steps in oxidative phosphorylation. Historically, the carrier was thought to form a homodimer and to operate by a sequential kinetic mechanism, which involves the formation of a ternary complex with the two exchanged substrates bound simultaneously. However, recent structural and functional data have demonstrated that the mitochondrial ADP/ATP carrier works as a monomer and has a single substrate binding site, which cannot be reconciled with a sequential kinetic mechanism. Here, we study the kinetic properties of the human mitochondrial ADP/ATP carrier by using proteoliposomes and transport robotics. We show that the Km/Vmax ratio is constant for all of the measured internal concentrations. Thus, in contrast to earlier claims, we conclude that the carrier operates with a ping‐pong kinetic mechanism in which substrate exchange across the membrane occurs consecutively rather than simultaneously. These data unite the kinetic and structural models, showing that the carrier operates with an alternating access mechanism.
Synopsis
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported.
The kinetics of the mitochondrial ADP/ATP carrier was studied using proteoliposomes and robotic transport assays.
Uptake curves were recorded to provide an accurate assessment of the initial transport rates in different substrate concentration gradients.
In two‐substrate initial‐velocity studies, the ratio of Km/Vmax is constant for all measured internal concentrations of the substrate.
The carrier operates with a ping‐pong kinetic mechanism in which the import and export transport steps occur consecutively.
Graphical Abstract
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported.</description><subject>Adenine</subject><subject>adenine nucleotide translocator</subject><subject>Adenine Nucleotide Translocator 1 - metabolism</subject><subject>Adenosine diphosphate</subject><subject>Adenosine Diphosphate - metabolism</subject><subject>Adenosine triphosphate</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>ADP/ATP translocase</subject><subject>ATP</subject><subject>Binding sites</subject><subject>Bioenergetics</subject><subject>Concentration gradient</subject><subject>Electron transport chain</subject><subject>EMBO20</subject><subject>EMBO21</subject><subject>EMBO57</subject><subject>Exchanging</subject><subject>Exports</subject><subject>Humans</subject><subject>Imports</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Ligands</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial ADP, ATP Translocases - chemistry</subject><subject>Mitochondrial ADP, ATP Translocases - metabolism</subject><subject>mitochondrial carrier family</subject><subject>Nucleotides</subject><subject>Oxidative phosphorylation</subject><subject>Phosphorylation</subject><subject>Robotics</subject><subject>SLC25</subject><subject>Structural models</subject><subject>Structure-function relationships</subject><subject>Substrates</subject><subject>Translocase</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNqFkc1uEzEURi0EoqWwZocssWGTxr9jDxuUhpYiBVFBkWBleZw7icuMPdgzrbrjEXhGnoQpCaEgIVa-ks93dK8-hB5Tckglk2wKbZUOGWFcKsrUHbRPRVFOOFX67nZmjH7cQw9yviCEyFLp-2iPK6Y0lXoffTodWhtw6_vo1jEsk7cNnr08m87Oz7CzKXlI-P1izuRM4NhBsj1kfOX7Nba482H1_eu3LoYV_uwD9N7hFtzaBp_bh-hebZsMj7bvAfpwcnw-P50s3r56PZ8tJk5SoSZVLWpGQNS24qCWAggUTDspLAW9BAWMlqzSYOsKirqWglRCOC5rYgmvKOMH6MXG2w1VC0sHoU-2MV3yrU3XJlpv_vwJfm1W8dJQwktdiHI0PNsaUvwyQO5N67ODprEB4pAN04wTwQuqRvTpX-hFHFIY7xspIQlVjN8IpxvKpZhzgnq3DSXmZ2_mpjez621MPLl9xI7_VdQIPN8AV76B6__5zPGbo3e37WQTzmMurCD93vpfC_0Adhi2Cw</recordid><startdate>20230803</startdate><enddate>20230803</enddate><creator>Cimadamore‐Werthein, Camila</creator><creator>Jaiquel Baron, Stephany</creator><creator>King, Martin S</creator><creator>Springett, Roger</creator><creator>Kunji, Edmund RS</creator><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>John Wiley and Sons Inc</general><scope>C6C</scope><scope>24P</scope><scope>WIN</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>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-6030-5154</orcidid><orcidid>https://orcid.org/0000-0002-0610-4500</orcidid><orcidid>https://orcid.org/0000-0001-5507-817X</orcidid></search><sort><creationdate>20230803</creationdate><title>Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping‐pong kinetic mechanism</title><author>Cimadamore‐Werthein, Camila ; Jaiquel Baron, Stephany ; King, Martin S ; Springett, Roger ; Kunji, Edmund RS</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5147-bf4f20e4fab3e7d4e0e628c54a1e8de7e2192b8eafbe6ff540b44c35f0a03b123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Adenine</topic><topic>adenine nucleotide translocator</topic><topic>Adenine Nucleotide Translocator 1 - metabolism</topic><topic>Adenosine diphosphate</topic><topic>Adenosine Diphosphate - metabolism</topic><topic>Adenosine triphosphate</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>ADP/ATP translocase</topic><topic>ATP</topic><topic>Binding sites</topic><topic>Bioenergetics</topic><topic>Concentration gradient</topic><topic>Electron transport chain</topic><topic>EMBO20</topic><topic>EMBO21</topic><topic>EMBO57</topic><topic>Exchanging</topic><topic>Exports</topic><topic>Humans</topic><topic>Imports</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Ligands</topic><topic>Mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial ADP, ATP Translocases - chemistry</topic><topic>Mitochondrial ADP, ATP Translocases - metabolism</topic><topic>mitochondrial carrier family</topic><topic>Nucleotides</topic><topic>Oxidative phosphorylation</topic><topic>Phosphorylation</topic><topic>Robotics</topic><topic>SLC25</topic><topic>Structural models</topic><topic>Structure-function relationships</topic><topic>Substrates</topic><topic>Translocase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cimadamore‐Werthein, Camila</creatorcontrib><creatorcontrib>Jaiquel Baron, Stephany</creatorcontrib><creatorcontrib>King, Martin S</creatorcontrib><creatorcontrib>Springett, Roger</creatorcontrib><creatorcontrib>Kunji, Edmund RS</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Wiley Online Library Open Access</collection><collection>Wiley Online Library Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cimadamore‐Werthein, Camila</au><au>Jaiquel Baron, Stephany</au><au>King, Martin S</au><au>Springett, Roger</au><au>Kunji, Edmund RS</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping‐pong kinetic mechanism</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2023-08-03</date><risdate>2023</risdate><volume>24</volume><issue>8</issue><spage>e57127</spage><epage>n/a</epage><pages>e57127-n/a</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><abstract>The mitochondrial ADP/ATP carrier (SLC25A4), also called the adenine nucleotide translocase, imports ADP into the mitochondrial matrix and exports ATP, which are key steps in oxidative phosphorylation. Historically, the carrier was thought to form a homodimer and to operate by a sequential kinetic mechanism, which involves the formation of a ternary complex with the two exchanged substrates bound simultaneously. However, recent structural and functional data have demonstrated that the mitochondrial ADP/ATP carrier works as a monomer and has a single substrate binding site, which cannot be reconciled with a sequential kinetic mechanism. Here, we study the kinetic properties of the human mitochondrial ADP/ATP carrier by using proteoliposomes and transport robotics. We show that the Km/Vmax ratio is constant for all of the measured internal concentrations. Thus, in contrast to earlier claims, we conclude that the carrier operates with a ping‐pong kinetic mechanism in which substrate exchange across the membrane occurs consecutively rather than simultaneously. These data unite the kinetic and structural models, showing that the carrier operates with an alternating access mechanism.
Synopsis
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported.
The kinetics of the mitochondrial ADP/ATP carrier was studied using proteoliposomes and robotic transport assays.
Uptake curves were recorded to provide an accurate assessment of the initial transport rates in different substrate concentration gradients.
In two‐substrate initial‐velocity studies, the ratio of Km/Vmax is constant for all measured internal concentrations of the substrate.
The carrier operates with a ping‐pong kinetic mechanism in which the import and export transport steps occur consecutively.
Graphical Abstract
The human mitochondrial ADP/ATP carrier (SLC25A4) operates with a ping‐pong kinetic mechanism in which one substrate is imported before the other substrate is exported.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>37278158</pmid><doi>10.15252/embr.202357127</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-6030-5154</orcidid><orcidid>https://orcid.org/0000-0002-0610-4500</orcidid><orcidid>https://orcid.org/0000-0001-5507-817X</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1469-221X |
| ispartof | EMBO reports, 2023-08, Vol.24 (8), p.e57127-n/a |
| issn | 1469-221X 1469-3178 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10398649 |
| source | MEDLINE; Wiley Journals; Wiley Online Library Free Content; Springer Nature OA Free Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Adenine adenine nucleotide translocator Adenine Nucleotide Translocator 1 - metabolism Adenosine diphosphate Adenosine Diphosphate - metabolism Adenosine triphosphate Adenosine Triphosphate - metabolism ADP/ATP translocase ATP Binding sites Bioenergetics Concentration gradient Electron transport chain EMBO20 EMBO21 EMBO57 Exchanging Exports Humans Imports Kinetics Life Sciences Ligands Mitochondria Mitochondria - metabolism Mitochondrial ADP, ATP Translocases - chemistry Mitochondrial ADP, ATP Translocases - metabolism mitochondrial carrier family Nucleotides Oxidative phosphorylation Phosphorylation Robotics SLC25 Structural models Structure-function relationships Substrates Translocase |
| title | Human mitochondrial ADP/ATP carrier SLC25A4 operates with a ping‐pong kinetic mechanism |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T00%3A53%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Human%20mitochondrial%20ADP/ATP%20carrier%20SLC25A4%20operates%20with%20a%20ping%E2%80%90pong%20kinetic%20mechanism&rft.jtitle=EMBO%20reports&rft.au=Cimadamore%E2%80%90Werthein,%20Camila&rft.date=2023-08-03&rft.volume=24&rft.issue=8&rft.spage=e57127&rft.epage=n/a&rft.pages=e57127-n/a&rft.issn=1469-221X&rft.eissn=1469-3178&rft_id=info:doi/10.15252/embr.202357127&rft_dat=%3Cproquest_pubme%3E2845017239%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2845017239&rft_id=info:pmid/37278158&rfr_iscdi=true |