Catalytic effect of riboflavin on electron transfer from NADH to aquacobalamin
Reduction of cobalamin by non-dedicated cellular reductases has been reported in earlier work, however, the sources of reducing power and the mechanisms are unknown. This study reports results of kinetic and mechanistic investigation of the reaction between aquacobalamin, H 2 OCbl, and reduced β-nic...
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| Veröffentlicht in: | Journal of biological inorganic chemistry 2020-02, Vol.25 (1), p.125-133 |
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| creator | Dereven’kov, Ilia A. Hannibal, Luciana Makarov, Sergei V. Molodtsov, Pavel A. |
| description | Reduction of cobalamin by non-dedicated cellular reductases has been reported in earlier work, however, the sources of reducing power and the mechanisms are unknown. This study reports results of kinetic and mechanistic investigation of the reaction between aquacobalamin, H
2
OCbl, and reduced β-nicotinamide adenine dinucleotide, NADH. This interaction leads to the formation of one-electron reduced cobalamin, cob(II)alamin, and proceeds via water substitution on aquacobalamin by NADH and further decomposition of NADH–Co(III) complex to cob(II)alamin and NADH
·
+
. Riboflavin catalyzes the reduction of aquacobalamin by NADH both in free form and with aquacobalamin bound to the cobalamin processing enzyme CblC. The rate-determining step of this catalytic reaction is the interaction between riboflavin and NADH to produce a charge transfer complex that reacts with aquacobalamin. Aquacobalamin quenches the fluorescence of NADH and riboflavin predominantly via a static mechanism.
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| doi_str_mv | 10.1007/s00775-019-01745-3 |
| format | Article |
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2
OCbl, and reduced β-nicotinamide adenine dinucleotide, NADH. This interaction leads to the formation of one-electron reduced cobalamin, cob(II)alamin, and proceeds via water substitution on aquacobalamin by NADH and further decomposition of NADH–Co(III) complex to cob(II)alamin and NADH
·
+
. Riboflavin catalyzes the reduction of aquacobalamin by NADH both in free form and with aquacobalamin bound to the cobalamin processing enzyme CblC. The rate-determining step of this catalytic reaction is the interaction between riboflavin and NADH to produce a charge transfer complex that reacts with aquacobalamin. Aquacobalamin quenches the fluorescence of NADH and riboflavin predominantly via a static mechanism.
Graphic abstract</description><identifier>ISSN: 0949-8257</identifier><identifier>EISSN: 1432-1327</identifier><identifier>DOI: 10.1007/s00775-019-01745-3</identifier><identifier>PMID: 31773269</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Adenine ; Biochemistry ; Biomedical and Life Sciences ; Catalysis ; Electron transfer ; Electron Transport - drug effects ; Fluorescence ; Humans ; Inorganic chemistry ; Life Sciences ; Microbiology ; NAD ; NAD - metabolism ; NADH ; Nicotinamide ; Original Paper ; Proto-Oncogene Proteins c-cbl - metabolism ; Riboflavin ; Riboflavin - pharmacology ; Spectrum Analysis ; Vitamin B ; Vitamin B 12 - analogs & derivatives ; Vitamin B 12 - metabolism ; Vitamin B12</subject><ispartof>Journal of biological inorganic chemistry, 2020-02, Vol.25 (1), p.125-133</ispartof><rights>Society for Biological Inorganic Chemistry (SBIC) 2019</rights><rights>2019© Society for Biological Inorganic Chemistry (SBIC) 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-9ca638e0b1a168c2eb78bc07bea898151f1e9cf475a86e5100123e30f720f2753</citedby><cites>FETCH-LOGICAL-c375t-9ca638e0b1a168c2eb78bc07bea898151f1e9cf475a86e5100123e30f720f2753</cites><orcidid>0000-0003-1332-4998 ; 0000-0002-0911-5758</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00775-019-01745-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00775-019-01745-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31773269$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dereven’kov, Ilia A.</creatorcontrib><creatorcontrib>Hannibal, Luciana</creatorcontrib><creatorcontrib>Makarov, Sergei V.</creatorcontrib><creatorcontrib>Molodtsov, Pavel A.</creatorcontrib><title>Catalytic effect of riboflavin on electron transfer from NADH to aquacobalamin</title><title>Journal of biological inorganic chemistry</title><addtitle>J Biol Inorg Chem</addtitle><addtitle>J Biol Inorg Chem</addtitle><description>Reduction of cobalamin by non-dedicated cellular reductases has been reported in earlier work, however, the sources of reducing power and the mechanisms are unknown. This study reports results of kinetic and mechanistic investigation of the reaction between aquacobalamin, H
2
OCbl, and reduced β-nicotinamide adenine dinucleotide, NADH. This interaction leads to the formation of one-electron reduced cobalamin, cob(II)alamin, and proceeds via water substitution on aquacobalamin by NADH and further decomposition of NADH–Co(III) complex to cob(II)alamin and NADH
·
+
. Riboflavin catalyzes the reduction of aquacobalamin by NADH both in free form and with aquacobalamin bound to the cobalamin processing enzyme CblC. The rate-determining step of this catalytic reaction is the interaction between riboflavin and NADH to produce a charge transfer complex that reacts with aquacobalamin. Aquacobalamin quenches the fluorescence of NADH and riboflavin predominantly via a static mechanism.
Graphic abstract</description><subject>Adenine</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Catalysis</subject><subject>Electron transfer</subject><subject>Electron Transport - drug effects</subject><subject>Fluorescence</subject><subject>Humans</subject><subject>Inorganic chemistry</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>NAD</subject><subject>NAD - metabolism</subject><subject>NADH</subject><subject>Nicotinamide</subject><subject>Original Paper</subject><subject>Proto-Oncogene Proteins c-cbl - metabolism</subject><subject>Riboflavin</subject><subject>Riboflavin - pharmacology</subject><subject>Spectrum Analysis</subject><subject>Vitamin B</subject><subject>Vitamin B 12 - analogs & derivatives</subject><subject>Vitamin B 12 - metabolism</subject><subject>Vitamin B12</subject><issn>0949-8257</issn><issn>1432-1327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kLtOwzAUhi0EoqXwAgzIEgtLwJc6jseqXIpUlQVmyzHHKFUSt3aC1LfHkAISA4Mvsr_z2-dD6JySa0qIvIlpkiIjVKUhpyLjB2hMp5xllDN5iMZETVVWMCFH6CTGNSGECyqO0YhTKTnL1Rit5qYz9a6rLAbnwHbYOxyq0rvavFct9i2GOh2HtOmCaaODgF3wDV7Nbhe489hse2N9aWrTVO0pOnKmjnC2Xyfo5f7ueb7Ilk8Pj_PZMrNcii5T1uS8AFJSQ_PCMihlUVoiSzCFKqigjoKybiqFKXIQqVvKOHDiJCOOScEn6GrI3QS_7SF2uqmihbo2Lfg-asapoip1SBJ6-Qdd-z606XeJkkLxPFd5othA2eBjDOD0JlSNCTtNif60rQfbOtnWX7Y1T0UX--i-bOD1p-RbbwL4AMR01b5B-H37n9gPDDuI1A</recordid><startdate>20200201</startdate><enddate>20200201</enddate><creator>Dereven’kov, Ilia A.</creator><creator>Hannibal, Luciana</creator><creator>Makarov, Sergei V.</creator><creator>Molodtsov, Pavel A.</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</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>7X8</scope><orcidid>https://orcid.org/0000-0003-1332-4998</orcidid><orcidid>https://orcid.org/0000-0002-0911-5758</orcidid></search><sort><creationdate>20200201</creationdate><title>Catalytic effect of riboflavin on electron transfer from NADH to aquacobalamin</title><author>Dereven’kov, Ilia A. ; Hannibal, Luciana ; Makarov, Sergei V. ; Molodtsov, Pavel A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-9ca638e0b1a168c2eb78bc07bea898151f1e9cf475a86e5100123e30f720f2753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Adenine</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Catalysis</topic><topic>Electron transfer</topic><topic>Electron Transport - drug effects</topic><topic>Fluorescence</topic><topic>Humans</topic><topic>Inorganic chemistry</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>NAD</topic><topic>NAD - metabolism</topic><topic>NADH</topic><topic>Nicotinamide</topic><topic>Original Paper</topic><topic>Proto-Oncogene Proteins c-cbl - metabolism</topic><topic>Riboflavin</topic><topic>Riboflavin - pharmacology</topic><topic>Spectrum Analysis</topic><topic>Vitamin B</topic><topic>Vitamin B 12 - analogs & derivatives</topic><topic>Vitamin B 12 - metabolism</topic><topic>Vitamin B12</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dereven’kov, Ilia A.</creatorcontrib><creatorcontrib>Hannibal, Luciana</creatorcontrib><creatorcontrib>Makarov, Sergei V.</creatorcontrib><creatorcontrib>Molodtsov, Pavel A.</creatorcontrib><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><jtitle>Journal of biological inorganic chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dereven’kov, Ilia A.</au><au>Hannibal, Luciana</au><au>Makarov, Sergei V.</au><au>Molodtsov, Pavel A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Catalytic effect of riboflavin on electron transfer from NADH to aquacobalamin</atitle><jtitle>Journal of biological inorganic chemistry</jtitle><stitle>J Biol Inorg Chem</stitle><addtitle>J Biol Inorg Chem</addtitle><date>2020-02-01</date><risdate>2020</risdate><volume>25</volume><issue>1</issue><spage>125</spage><epage>133</epage><pages>125-133</pages><issn>0949-8257</issn><eissn>1432-1327</eissn><abstract>Reduction of cobalamin by non-dedicated cellular reductases has been reported in earlier work, however, the sources of reducing power and the mechanisms are unknown. This study reports results of kinetic and mechanistic investigation of the reaction between aquacobalamin, H
2
OCbl, and reduced β-nicotinamide adenine dinucleotide, NADH. This interaction leads to the formation of one-electron reduced cobalamin, cob(II)alamin, and proceeds via water substitution on aquacobalamin by NADH and further decomposition of NADH–Co(III) complex to cob(II)alamin and NADH
·
+
. Riboflavin catalyzes the reduction of aquacobalamin by NADH both in free form and with aquacobalamin bound to the cobalamin processing enzyme CblC. The rate-determining step of this catalytic reaction is the interaction between riboflavin and NADH to produce a charge transfer complex that reacts with aquacobalamin. Aquacobalamin quenches the fluorescence of NADH and riboflavin predominantly via a static mechanism.
Graphic abstract</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>31773269</pmid><doi>10.1007/s00775-019-01745-3</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-1332-4998</orcidid><orcidid>https://orcid.org/0000-0002-0911-5758</orcidid></addata></record> |
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| subjects | Adenine Biochemistry Biomedical and Life Sciences Catalysis Electron transfer Electron Transport - drug effects Fluorescence Humans Inorganic chemistry Life Sciences Microbiology NAD NAD - metabolism NADH Nicotinamide Original Paper Proto-Oncogene Proteins c-cbl - metabolism Riboflavin Riboflavin - pharmacology Spectrum Analysis Vitamin B Vitamin B 12 - analogs & derivatives Vitamin B 12 - metabolism Vitamin B12 |
| title | Catalytic effect of riboflavin on electron transfer from NADH to aquacobalamin |
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