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Splitting of the O-O bond at the heme-copper catalytic site of respiratory oxidases
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för organisk kemi.
Vise andre og tillknytning
Rekke forfattare: 62017 (engelsk)Inngår i: Science Advances, ISSN 0036-8156, E-ISSN 2375-2548, Vol. 3, nr 6, artikkel-id e1700279Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Heme-copper oxidases catalyze the four-electron reduction of O-2 to H2O at a catalytic site that is composed of a heme group, a copper ion (Cu-B), and a tyrosine residue. Results from earlier experimental studies have shown that the O-O bond is cleaved simultaneously with electron transfer from a low-spin heme (heme a/b), forming a ferryl state (P-R; Fe4+= O2-, Cu-B(2+)-OH-). We show that with the Thermus thermophilus ba(3) oxidase, at low temperature (10 degrees C, pH 7), electron transfer from the low-spin heme b to the catalytic site is faster by a factor of similar to 10 (tau congruent to 11 mu s) than the formation of the P-R ferryl (t. 110 ms), which indicates that O-2 is reduced before the splitting of the O-O bond. Application of density functional theory indicates that the electron acceptor at the catalytic site is a high-energy peroxy state [Fe3+-O--O-(H+)], which is formed before the P-R ferryl. The rates of heme b oxidation and P-R ferryl formation were more similar at pH 10, indicating that the formation of the high-energy peroxy state involves proton transfer within the catalytic site, consistent with theory. The combined experimental and theoretical data suggest a general mechanism for O-2 reduction by heme-copper oxidases.

sted, utgiver, år, opplag, sider
2017. Vol. 3, nr 6, artikkel-id e1700279
HSV kategori
Forskningsprogram
biokemi
Identifikatorer
URN: urn:nbn:se:su:diva-147192DOI: 10.1126/sciadv.1700279ISI: 000406370700061OAI: oai:DiVA.org:su-147192DiVA, id: diva2:1142931
Tilgjengelig fra: 2017-09-20 Laget: 2017-09-20 Sist oppdatert: 2017-09-21bibliografisk kontrollert

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