Loading…

Assembly of functional b-type cytochromes in membranes from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli

It is the aim of this study to investigate which cytochromes are reconstituted during incubation of haemdeficient membranes with haematin and ATP. The reconstituted cytochromes have been studied by potentiometric redox titrations and low-temperature spectrophotometry of membrane preparations, and co...

Full description

Saved in:

Bibliographic Details
Published in:	FEBS letters 1981-08, Vol.131 (2), p.346-350
Main Authors:	Reid, Graeme A., Haddock, Bruce A., Ingledew, W.John
Format:	Article
Language:	English
Subjects:	Adenosine Triphosphate - metabolism Aminolevulinic Acid - metabolism ATP Cell Membrane - metabolism Cytochrome b Group cytochromes Cytochromes - metabolism Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Heme - analogs & derivatives Heme - deficiency Hemin - metabolism Levulinic Acids - metabolism membranes Multienzyme Complexes - metabolism NADH, NADPH Oxidoreductases - metabolism Oxidation-Reduction reconstitution Spectrophotometry
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by	cdi_FETCH-LOGICAL-c4970-bf41ba01fd21588e655225f75b345132876df2dd3907047dcd6e13013b5d04123
cites	cdi_FETCH-LOGICAL-c4970-bf41ba01fd21588e655225f75b345132876df2dd3907047dcd6e13013b5d04123
container_end_page	350
container_issue	2
container_start_page	346
container_title	FEBS letters
container_volume	131
creator	Reid, Graeme A. Haddock, Bruce A. Ingledew, W.John
description	It is the aim of this study to investigate which cytochromes are reconstituted during incubation of haemdeficient membranes with haematin and ATP. The reconstituted cytochromes have been studied by potentiometric redox titrations and low-temperature spectrophotometry of membrane preparations, and compared with the cytochromes found in prototrophic E. coli . The requirement for ATP during reconstitution has been further investigated by similar studies with haem-deficient membranes which had been incubated with haematin in the absence of ATP; cytochromes are apparently reconstituted but these membranes lack NADH oxidase activity.
doi_str_mv	10.1016/0014-5793(81)80400-0
format	article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_73742741</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0014579381804000</els_id><sourcerecordid>73742741</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4970-bf41ba01fd21588e655225f75b345132876df2dd3907047dcd6e13013b5d04123</originalsourceid><addsrcrecordid>eNqNUcFu1DAUtBCoLIU_AMknBIe0frEdOxekttqFSpW4lLPl2C-sURJv7aQof0_SXfUInKw3M29szxDyHtgFMKguGQNRSFXzTxo-ayYYK9gLsgGteMFFpV-SzbPkNXmT8y-2zBrqM3KmWKklqzdkvsoZ-6abaWxpOw1uDHGwHW2KcT4gdfMY3T7FHjMNA-0XabLDMrQLRi2Vhe3DEDuLj1MXhuCodcEXCR-mkMLwk_bTaIdxNd9mt8cU3D5Y6mIX3pJXre0yvjud5-THbnt_8624-_719ubqrnCiVqxoWgGNZdD6EqTWWElZlrJVsuFCAi-1qnxbes9rpphQ3vkKgTPgjfRMQMnPycej7yHFhwnzaPqQHXbd8o84ZaO4EqUS8E8hSCFEVa2O4ih0KeacsDWHFHqbZgPMrNWYNXez5m40mKdqDFvWPpz8p6ZH_7x06mLhd0f-d-hw_i9Ps9telyux4hqe0PWiL0cjXGJ9DJhMdgEHhz4kdKPxMfz9pX8AWCmwpQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15444662</pqid></control><display><type>article</type><title>Assembly of functional b-type cytochromes in membranes from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli</title><source>ScienceDirect®</source><creator>Reid, Graeme A. ; Haddock, Bruce A. ; Ingledew, W.John</creator><creatorcontrib>Reid, Graeme A. ; Haddock, Bruce A. ; Ingledew, W.John</creatorcontrib><description>It is the aim of this study to investigate which cytochromes are reconstituted during incubation of haemdeficient membranes with haematin and ATP. The reconstituted cytochromes have been studied by potentiometric redox titrations and low-temperature spectrophotometry of membrane preparations, and compared with the cytochromes found in prototrophic E. coli . The requirement for ATP during reconstitution has been further investigated by similar studies with haem-deficient membranes which had been incubated with haematin in the absence of ATP; cytochromes are apparently reconstituted but these membranes lack NADH oxidase activity.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(81)80400-0</identifier><identifier>PMID: 7028509</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Adenosine Triphosphate - metabolism ; Aminolevulinic Acid - metabolism ; ATP ; Cell Membrane - metabolism ; Cytochrome b Group ; cytochromes ; Cytochromes - metabolism ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Heme - analogs & derivatives ; Heme - deficiency ; Hemin - metabolism ; Levulinic Acids - metabolism ; membranes ; Multienzyme Complexes - metabolism ; NADH, NADPH Oxidoreductases - metabolism ; Oxidation-Reduction ; reconstitution ; Spectrophotometry</subject><ispartof>FEBS letters, 1981-08, Vol.131 (2), p.346-350</ispartof><rights>1981</rights><rights>FEBS Letters 131 (1981) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4970-bf41ba01fd21588e655225f75b345132876df2dd3907047dcd6e13013b5d04123</citedby><cites>FETCH-LOGICAL-c4970-bf41ba01fd21588e655225f75b345132876df2dd3907047dcd6e13013b5d04123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579381804000$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7028509$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reid, Graeme A.</creatorcontrib><creatorcontrib>Haddock, Bruce A.</creatorcontrib><creatorcontrib>Ingledew, W.John</creatorcontrib><title>Assembly of functional b-type cytochromes in membranes from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>It is the aim of this study to investigate which cytochromes are reconstituted during incubation of haemdeficient membranes with haematin and ATP. The reconstituted cytochromes have been studied by potentiometric redox titrations and low-temperature spectrophotometry of membrane preparations, and compared with the cytochromes found in prototrophic E. coli . The requirement for ATP during reconstitution has been further investigated by similar studies with haem-deficient membranes which had been incubated with haematin in the absence of ATP; cytochromes are apparently reconstituted but these membranes lack NADH oxidase activity.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Aminolevulinic Acid - metabolism</subject><subject>ATP</subject><subject>Cell Membrane - metabolism</subject><subject>Cytochrome b Group</subject><subject>cytochromes</subject><subject>Cytochromes - metabolism</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Heme - analogs & derivatives</subject><subject>Heme - deficiency</subject><subject>Hemin - metabolism</subject><subject>Levulinic Acids - metabolism</subject><subject>membranes</subject><subject>Multienzyme Complexes - metabolism</subject><subject>NADH, NADPH Oxidoreductases - metabolism</subject><subject>Oxidation-Reduction</subject><subject>reconstitution</subject><subject>Spectrophotometry</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><recordid>eNqNUcFu1DAUtBCoLIU_AMknBIe0frEdOxekttqFSpW4lLPl2C-sURJv7aQof0_SXfUInKw3M29szxDyHtgFMKguGQNRSFXzTxo-ayYYK9gLsgGteMFFpV-SzbPkNXmT8y-2zBrqM3KmWKklqzdkvsoZ-6abaWxpOw1uDHGwHW2KcT4gdfMY3T7FHjMNA-0XabLDMrQLRi2Vhe3DEDuLj1MXhuCodcEXCR-mkMLwk_bTaIdxNd9mt8cU3D5Y6mIX3pJXre0yvjud5-THbnt_8624-_719ubqrnCiVqxoWgGNZdD6EqTWWElZlrJVsuFCAi-1qnxbes9rpphQ3vkKgTPgjfRMQMnPycej7yHFhwnzaPqQHXbd8o84ZaO4EqUS8E8hSCFEVa2O4ih0KeacsDWHFHqbZgPMrNWYNXez5m40mKdqDFvWPpz8p6ZH_7x06mLhd0f-d-hw_i9Ps9telyux4hqe0PWiL0cjXGJ9DJhMdgEHhz4kdKPxMfz9pX8AWCmwpQ</recordid><startdate>19810831</startdate><enddate>19810831</enddate><creator>Reid, Graeme A.</creator><creator>Haddock, Bruce A.</creator><creator>Ingledew, W.John</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19810831</creationdate><title>Assembly of functional b-type cytochromes in membranes from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli</title><author>Reid, Graeme A. ; Haddock, Bruce A. ; Ingledew, W.John</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4970-bf41ba01fd21588e655225f75b345132876df2dd3907047dcd6e13013b5d04123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Aminolevulinic Acid - metabolism</topic><topic>ATP</topic><topic>Cell Membrane - metabolism</topic><topic>Cytochrome b Group</topic><topic>cytochromes</topic><topic>Cytochromes - metabolism</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Heme - analogs & derivatives</topic><topic>Heme - deficiency</topic><topic>Hemin - metabolism</topic><topic>Levulinic Acids - metabolism</topic><topic>membranes</topic><topic>Multienzyme Complexes - metabolism</topic><topic>NADH, NADPH Oxidoreductases - metabolism</topic><topic>Oxidation-Reduction</topic><topic>reconstitution</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reid, Graeme A.</creatorcontrib><creatorcontrib>Haddock, Bruce A.</creatorcontrib><creatorcontrib>Ingledew, W.John</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reid, Graeme A.</au><au>Haddock, Bruce A.</au><au>Ingledew, W.John</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Assembly of functional b-type cytochromes in membranes from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1981-08-31</date><risdate>1981</risdate><volume>131</volume><issue>2</issue><spage>346</spage><epage>350</epage><pages>346-350</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>It is the aim of this study to investigate which cytochromes are reconstituted during incubation of haemdeficient membranes with haematin and ATP. The reconstituted cytochromes have been studied by potentiometric redox titrations and low-temperature spectrophotometry of membrane preparations, and compared with the cytochromes found in prototrophic E. coli . The requirement for ATP during reconstitution has been further investigated by similar studies with haem-deficient membranes which had been incubated with haematin in the absence of ATP; cytochromes are apparently reconstituted but these membranes lack NADH oxidase activity.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7028509</pmid><doi>10.1016/0014-5793(81)80400-0</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
fulltext	fulltext
identifier	ISSN: 0014-5793
ispartof	FEBS letters, 1981-08, Vol.131 (2), p.346-350
issn	0014-5793 1873-3468
language	eng
recordid	cdi_proquest_miscellaneous_73742741
source	ScienceDirect®
subjects	Adenosine Triphosphate - metabolism Aminolevulinic Acid - metabolism ATP Cell Membrane - metabolism Cytochrome b Group cytochromes Cytochromes - metabolism Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Heme - analogs & derivatives Heme - deficiency Hemin - metabolism Levulinic Acids - metabolism membranes Multienzyme Complexes - metabolism NADH, NADPH Oxidoreductases - metabolism Oxidation-Reduction reconstitution Spectrophotometry
title	Assembly of functional b-type cytochromes in membranes from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T16%3A27%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Assembly%20of%20functional%20b-type%20cytochromes%20in%20membranes%20from%20a%205-aminolaevulinic%20acid-requiring%20mutant%20of%20Escherichia%20coli&rft.jtitle=FEBS%20letters&rft.au=Reid,%20Graeme%20A.&rft.date=1981-08-31&rft.volume=131&rft.issue=2&rft.spage=346&rft.epage=350&rft.pages=346-350&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/0014-5793(81)80400-0&rft_dat=%3Cproquest_cross%3E73742741%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c4970-bf41ba01fd21588e655225f75b345132876df2dd3907047dcd6e13013b5d04123%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=15444662&rft_id=info:pmid/7028509&rfr_iscdi=true