Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli
In order to clarify the role of cytochrome in nitrate reductase we have performed spectrophotometric and stopped‐flow kinetic studies of reduction and oxidation of the cytochrome hemes with analogues of physiological quinones, using menadione as an analogue of menaquinone and duroquinone as an analo...
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| Veröffentlicht in: | European journal of biochemistry 2004-06, Vol.271 (12), p.2400-2407 |
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| container_title | European journal of biochemistry |
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| creator | Giordani, Roger Buc, Jean |
| description | In order to clarify the role of cytochrome in nitrate reductase we have performed spectrophotometric and stopped‐flow kinetic studies of reduction and oxidation of the cytochrome hemes with analogues of physiological quinones, using menadione as an analogue of menaquinone and duroquinone as an analogue of ubiquinone, and comparing the results with those obtained with dithionite. The spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete. Stopped‐flow kinetics of heme oxidation by potassium nitrate indicates that there are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. These results, and those of spectrophotometric studies of a mutant lacking the highest‐potential [Fe‐S] cluster, allow us to propose a two‐pathway electron transfer model for nitrate reductase A from Escherichia coli. |
| doi_str_mv | 10.1111/j.1432-1033.2004.04159.x |
| format | Article |
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The spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete. Stopped‐flow kinetics of heme oxidation by potassium nitrate indicates that there are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. 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The spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete. Stopped‐flow kinetics of heme oxidation by potassium nitrate indicates that there are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. These results, and those of spectrophotometric studies of a mutant lacking the highest‐potential [Fe‐S] cluster, allow us to propose a two‐pathway electron transfer model for nitrate reductase A from Escherichia coli.</description><subject>Benzoquinones - chemistry</subject><subject>Benzoquinones - metabolism</subject><subject>Cytochromes - chemistry</subject><subject>cytochrome b</subject><subject>Dithionite - chemistry</subject><subject>Dithionite - metabolism</subject><subject>electron transfer</subject><subject>Electron Transport</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Heme - chemistry</subject><subject>Nitrate Reductase</subject><subject>Nitrate Reductases - chemistry</subject><subject>Nitrate Reductases - metabolism</subject><subject>nitrate reductase A</subject><subject>Oxidation-Reduction</subject><subject>quinone</subject><subject>Spectrum Analysis</subject><subject>Vitamin K 3 - chemistry</subject><subject>Vitamin K 3 - metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkclOwzAQQC0EomX5BeQTJxK8Ns0FCVBZpEocgLPlOBPVVZZiJ7TlhMSf8iU4tIIjzGVG4zdjaR5CmJKYhjifx1RwFlHCecwIETERVKbxagcNfx520ZAQKiKWytEAHXg_J4SM0lGyjwZU0jHjUg5RN3m1OdQGcNE43C4bnNuiAAd1i6EE07qmxq3TtQ9NvNDtbKnXHtvQnAH2ugIM9du6gjNc28C1gB3knWm1h8_3j0tcuKbCE29m4KyZWY1NU9ojtFfo0sPxNh-i55vJ0_VdNH24vb--nEZGiCSNZMI41ZJQkhU5yzPQCeU0TzOacckM00yaLGSQvDB6rFMDWcolAaGllCPgh-h0s3fhmpcOfKsq6w2Upa6h6bxKwvG4EOxPkI7D7VjCAzjegMY13jso1MLZSru1okT1btRc9QpUr0D1btS3G7UKoyfbP7qsgvx3cCsjABcbYGlLWP97sbqZXD32Jf8CpR2ftQ</recordid><startdate>200406</startdate><enddate>200406</enddate><creator>Giordani, Roger</creator><creator>Buc, Jean</creator><general>Blackwell Science Ltd</general><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>C1K</scope><scope>7X8</scope></search><sort><creationdate>200406</creationdate><title>Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli</title><author>Giordani, Roger ; Buc, Jean</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4479-57231a5010bfd2dbea7131d9b1b352c2a25cb2c2e53fca8a9ceb9350e4a5556e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Benzoquinones - chemistry</topic><topic>Benzoquinones - metabolism</topic><topic>Cytochromes - chemistry</topic><topic>cytochrome b</topic><topic>Dithionite - chemistry</topic><topic>Dithionite - metabolism</topic><topic>electron transfer</topic><topic>Electron Transport</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Heme - chemistry</topic><topic>Nitrate Reductase</topic><topic>Nitrate Reductases - chemistry</topic><topic>Nitrate Reductases - metabolism</topic><topic>nitrate reductase A</topic><topic>Oxidation-Reduction</topic><topic>quinone</topic><topic>Spectrum Analysis</topic><topic>Vitamin K 3 - chemistry</topic><topic>Vitamin K 3 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Giordani, Roger</creatorcontrib><creatorcontrib>Buc, Jean</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Giordani, Roger</au><au>Buc, Jean</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>2004-06</date><risdate>2004</risdate><volume>271</volume><issue>12</issue><spage>2400</spage><epage>2407</epage><pages>2400-2407</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>In order to clarify the role of cytochrome in nitrate reductase we have performed spectrophotometric and stopped‐flow kinetic studies of reduction and oxidation of the cytochrome hemes with analogues of physiological quinones, using menadione as an analogue of menaquinone and duroquinone as an analogue of ubiquinone, and comparing the results with those obtained with dithionite. The spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete. Stopped‐flow kinetics of heme oxidation by potassium nitrate indicates that there are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. These results, and those of spectrophotometric studies of a mutant lacking the highest‐potential [Fe‐S] cluster, allow us to propose a two‐pathway electron transfer model for nitrate reductase A from Escherichia coli.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15182355</pmid><doi>10.1111/j.1432-1033.2004.04159.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 2004-06, Vol.271 (12), p.2400-2407 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Benzoquinones - chemistry Benzoquinones - metabolism Cytochromes - chemistry cytochrome b Dithionite - chemistry Dithionite - metabolism electron transfer Electron Transport Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Heme - chemistry Nitrate Reductase Nitrate Reductases - chemistry Nitrate Reductases - metabolism nitrate reductase A Oxidation-Reduction quinone Spectrum Analysis Vitamin K 3 - chemistry Vitamin K 3 - metabolism |
| title | Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli |
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