Individual heme a and heme a 3 contributions to the Soret absorption spectrum of the reduced bovine cytochrome c oxidase
Bovine cytochrome c oxidase (CcO) contains two hemes, a and a , chemically identical but differing in coordination and spin state. The Soret absorption band of reduced aa -type cytochrome c oxidase consists of overlapping bands of the hemes a and a . It shows a peak at ∼444 nm and a distinct shoulde...
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| Veröffentlicht in: | Biochimica et biophysica acta. Bioenergetics 2023-04, Vol.1864 (2), p.148937 |
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| container_title | Biochimica et biophysica acta. Bioenergetics |
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| creator | Diuba, Artem V Vygodina, Tatiana V Azarkina, Natalia V Arutyunyan, Alexander M Soulimane, Tewfik Vos, Marten H Konstantinov, Alexander A |
| description | Bovine cytochrome c oxidase (CcO) contains two hemes, a and a
, chemically identical but differing in coordination and spin state. The Soret absorption band of reduced aa
-type cytochrome c oxidase consists of overlapping bands of the hemes a
and a
. It shows a peak at ∼444 nm and a distinct shoulder at ∼425 nm. However, attribution of individual spectral lineshapes to hemes a
and a
in the Soret is controversial. In the present work, we characterized spectral contributions of hemes a
and a
using two approaches. First, we reconstructed bovine CcO heme a
spectrum using a selective Ca
-induced spectral shift of the heme a
. Second, we investigated photobleaching of the reduced Thermus thermophilus ba
- and bovine aa
-oxidases in the Soret induced by femtosecond laser pulses in the Q-band. The resolved spectra show splitting of the electronic B
-, B
-transitions of both reduced hemes. The heme a
spectrum is shifted to the red relative to heme a
spectrum. The ∼425 nm shoulder is mostly attributed to heme a
. |
| doi_str_mv | 10.1016/j.bbabio.2022.148937 |
| format | Article |
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, chemically identical but differing in coordination and spin state. The Soret absorption band of reduced aa
-type cytochrome c oxidase consists of overlapping bands of the hemes a
and a
. It shows a peak at ∼444 nm and a distinct shoulder at ∼425 nm. However, attribution of individual spectral lineshapes to hemes a
and a
in the Soret is controversial. In the present work, we characterized spectral contributions of hemes a
and a
using two approaches. First, we reconstructed bovine CcO heme a
spectrum using a selective Ca
-induced spectral shift of the heme a
. Second, we investigated photobleaching of the reduced Thermus thermophilus ba
- and bovine aa
-oxidases in the Soret induced by femtosecond laser pulses in the Q-band. The resolved spectra show splitting of the electronic B
-, B
-transitions of both reduced hemes. The heme a
spectrum is shifted to the red relative to heme a
spectrum. The ∼425 nm shoulder is mostly attributed to heme a
.</description><identifier>EISSN: 1879-2650</identifier><identifier>DOI: 10.1016/j.bbabio.2022.148937</identifier><identifier>PMID: 36403793</identifier><language>eng</language><publisher>Netherlands</publisher><subject>Animals ; Cattle ; Electron Transport Complex IV - metabolism ; Heme - metabolism ; Oxidation-Reduction ; Oxidoreductases - metabolism</subject><ispartof>Biochimica et biophysica acta. Bioenergetics, 2023-04, Vol.1864 (2), p.148937</ispartof><rights>Copyright © 2022 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36403793$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Diuba, Artem V</creatorcontrib><creatorcontrib>Vygodina, Tatiana V</creatorcontrib><creatorcontrib>Azarkina, Natalia V</creatorcontrib><creatorcontrib>Arutyunyan, Alexander M</creatorcontrib><creatorcontrib>Soulimane, Tewfik</creatorcontrib><creatorcontrib>Vos, Marten H</creatorcontrib><creatorcontrib>Konstantinov, Alexander A</creatorcontrib><title>Individual heme a and heme a 3 contributions to the Soret absorption spectrum of the reduced bovine cytochrome c oxidase</title><title>Biochimica et biophysica acta. Bioenergetics</title><addtitle>Biochim Biophys Acta Bioenerg</addtitle><description>Bovine cytochrome c oxidase (CcO) contains two hemes, a and a
, chemically identical but differing in coordination and spin state. The Soret absorption band of reduced aa
-type cytochrome c oxidase consists of overlapping bands of the hemes a
and a
. It shows a peak at ∼444 nm and a distinct shoulder at ∼425 nm. However, attribution of individual spectral lineshapes to hemes a
and a
in the Soret is controversial. In the present work, we characterized spectral contributions of hemes a
and a
using two approaches. First, we reconstructed bovine CcO heme a
spectrum using a selective Ca
-induced spectral shift of the heme a
. Second, we investigated photobleaching of the reduced Thermus thermophilus ba
- and bovine aa
-oxidases in the Soret induced by femtosecond laser pulses in the Q-band. The resolved spectra show splitting of the electronic B
-, B
-transitions of both reduced hemes. The heme a
spectrum is shifted to the red relative to heme a
spectrum. The ∼425 nm shoulder is mostly attributed to heme a
.</description><subject>Animals</subject><subject>Cattle</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Heme - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - metabolism</subject><issn>1879-2650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFjstqAkEURBshqEn8gyD3B5z0YzLjrEOCWZu99OPKtDh9h36I_n1M0HVWdaAORTH2IngluGheD5Ux2niqJJeyEvW6U-2EzcW67VayeeMz9pjSgV_VWqopm6mm5qrt1Jydv4LzJ--KPkKPA4IGHdwdFVgKOXpTsqeQIBPkHmFLETNokyiOvwWkEW2OZQDa_wkRXbHowNDJBwR7yWT7SNdNC3T2Tid8Zg97fUy4uOUTW35-fL9vVmMxA7rdGP2g42V3v6r-FX4AIrhR-w</recordid><startdate>20230401</startdate><enddate>20230401</enddate><creator>Diuba, Artem V</creator><creator>Vygodina, Tatiana V</creator><creator>Azarkina, Natalia V</creator><creator>Arutyunyan, Alexander M</creator><creator>Soulimane, Tewfik</creator><creator>Vos, Marten H</creator><creator>Konstantinov, Alexander A</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20230401</creationdate><title>Individual heme a and heme a 3 contributions to the Soret absorption spectrum of the reduced bovine cytochrome c oxidase</title><author>Diuba, Artem V ; Vygodina, Tatiana V ; Azarkina, Natalia V ; Arutyunyan, Alexander M ; Soulimane, Tewfik ; Vos, Marten H ; Konstantinov, Alexander A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-pubmed_primary_364037933</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Electron Transport Complex IV - metabolism</topic><topic>Heme - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Diuba, Artem V</creatorcontrib><creatorcontrib>Vygodina, Tatiana V</creatorcontrib><creatorcontrib>Azarkina, Natalia V</creatorcontrib><creatorcontrib>Arutyunyan, Alexander M</creatorcontrib><creatorcontrib>Soulimane, Tewfik</creatorcontrib><creatorcontrib>Vos, Marten H</creatorcontrib><creatorcontrib>Konstantinov, Alexander A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Biochimica et biophysica acta. Bioenergetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Diuba, Artem V</au><au>Vygodina, Tatiana V</au><au>Azarkina, Natalia V</au><au>Arutyunyan, Alexander M</au><au>Soulimane, Tewfik</au><au>Vos, Marten H</au><au>Konstantinov, Alexander A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Individual heme a and heme a 3 contributions to the Soret absorption spectrum of the reduced bovine cytochrome c oxidase</atitle><jtitle>Biochimica et biophysica acta. Bioenergetics</jtitle><addtitle>Biochim Biophys Acta Bioenerg</addtitle><date>2023-04-01</date><risdate>2023</risdate><volume>1864</volume><issue>2</issue><spage>148937</spage><pages>148937-</pages><eissn>1879-2650</eissn><abstract>Bovine cytochrome c oxidase (CcO) contains two hemes, a and a
, chemically identical but differing in coordination and spin state. The Soret absorption band of reduced aa
-type cytochrome c oxidase consists of overlapping bands of the hemes a
and a
. It shows a peak at ∼444 nm and a distinct shoulder at ∼425 nm. However, attribution of individual spectral lineshapes to hemes a
and a
in the Soret is controversial. In the present work, we characterized spectral contributions of hemes a
and a
using two approaches. First, we reconstructed bovine CcO heme a
spectrum using a selective Ca
-induced spectral shift of the heme a
. Second, we investigated photobleaching of the reduced Thermus thermophilus ba
- and bovine aa
-oxidases in the Soret induced by femtosecond laser pulses in the Q-band. The resolved spectra show splitting of the electronic B
-, B
-transitions of both reduced hemes. The heme a
spectrum is shifted to the red relative to heme a
spectrum. The ∼425 nm shoulder is mostly attributed to heme a
.</abstract><cop>Netherlands</cop><pmid>36403793</pmid><doi>10.1016/j.bbabio.2022.148937</doi></addata></record> |
| fulltext | fulltext |
| identifier | EISSN: 1879-2650 |
| ispartof | Biochimica et biophysica acta. Bioenergetics, 2023-04, Vol.1864 (2), p.148937 |
| issn | 1879-2650 |
| language | eng |
| recordid | cdi_pubmed_primary_36403793 |
| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Cattle Electron Transport Complex IV - metabolism Heme - metabolism Oxidation-Reduction Oxidoreductases - metabolism |
| title | Individual heme a and heme a 3 contributions to the Soret absorption spectrum of the reduced bovine cytochrome c oxidase |
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