A new route to carbon monoxide adducts of heme proteins

作者：Makarov Sergei V^*; Salnikov Denis S; Pogorelova Anna S; Kis Zoltan; Silaghi Dumitrescu Radu

来源：Journal of Porphyrins and Phthalocyanines, 2008, 12(10): 1096-1099.

• myoglobin
• hemoglobin
• heme
• carbon monoxide
• dithionite
• sulfoxylate
• thiourea dioxide

Sulfoxylate SO(2)H(-) (SO(2)(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 CO(2) 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.

• 出版日期2008