A new route to carbon monoxide adducts of HEME proteins
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MACAROV, Serghei, SALNIKOV, Denis, POGORELOVA, Anna, KISC, Zoltan, SILAGHI-DUMITRESCU, Radu. A new route to carbon monoxide adducts of HEME proteins. In: International Conference of Young Researchers , 6-7 noiembrie 2008, Chişinău. Chişinău: Tipogr. Simbol-NP SRL, 2008, Ediția 6, p. 80. ISBN 978-9975-70-769-5.
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International Conference of Young Researchers
Ediția 6, 2008
Conferința "International Conference of Young Researchers "
Chişinău, Moldova, 6-7 noiembrie 2008

A new route to carbon monoxide adducts of HEME proteins


Pag. 80-80

Macarov Serghei1, Salnikov Denis1, Pogorelova Anna1, Kisc Zoltan2, Silaghi-Dumitrescu Radu2
 
1 Ivanovo State University of Chemistry and Technology,
2 Babeș-Bolyai University
 
 
Disponibil în IBN: 25 mai 2021


Rezumat

Sulfoxylate SO2H- (SO2 2-), a strong reducing agent readily produced by hydrolysis of thiourea dioxide, reacts with ferric myoglobin (Mb) to reversibly produce Fe(II)-Mb, starting from either aerobic or anaerobic conditions. Exposure of Fe(II)-Mb to excess sulfoxylate further produces Fe(II)-CO-Mb. Fe(II)-Mb can be regenerated by reoxidation with ferricyanide at this stage; hemin, rubredoxin and cytochrome c show a similar reactivity towards sulfoxylate. The source of CO is not the protein moiety, nor is it the heme or the thiourea dioxide – but rather CO2, via its reaction with sulfoxylate when the latter is used in large excess. These findings provide a convenient single-step route to carbon monoxide heme adducts, without the need to manipulate toxic CO gas. Financial support from the Romanian Ministry of Education and Research, (CEEx-ET98/2006, to RSD), Russian Foundation for Basic Research and Romanian Academy (joint grant to RSD and SVM), and “Babes-Bolyai” University (Scholarship for Scientific Research to KZ) is gratefully acknowledged.

Cuvinte-cheie
myoglobin, Hemoglobin, heme, Carbon monoxide, dithionite, sulfoxylate, thiourea dioxide

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<subjects>
<subject>myoglobin</subject>
<subject>Hemoglobin</subject>
<subject>heme</subject>
<subject>Carbon monoxide</subject>
<subject>dithionite</subject>
<subject>sulfoxylate</subject>
<subject>thiourea dioxide</subject>
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<description xml:lang='en' descriptionType='Abstract'><p>Sulfoxylate SO2H- (SO2 2-), a strong reducing agent readily produced by hydrolysis of thiourea dioxide, reacts with ferric myoglobin (Mb) to reversibly produce Fe(II)-Mb, starting from either aerobic or anaerobic conditions. Exposure of Fe(II)-Mb to excess sulfoxylate further produces Fe(II)-CO-Mb. Fe(II)-Mb can be regenerated by reoxidation with ferricyanide at this stage; hemin, rubredoxin and cytochrome c show a similar reactivity towards sulfoxylate. The source of CO is not the protein moiety, nor is it the heme or the thiourea dioxide &ndash; but rather CO2, via its reaction with sulfoxylate when the latter is used in large excess. These findings provide a convenient single-step route to carbon monoxide heme adducts, without the need to manipulate toxic CO gas. Financial support from the Romanian Ministry of Education and Research, (CEEx-ET98/2006, to RSD), Russian Foundation for Basic Research and Romanian Academy (joint grant to RSD and SVM), and &ldquo;Babes-Bolyai&rdquo; University (Scholarship for Scientific Research to KZ) is gratefully acknowledged.</p></description>
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