Photochemical processes observed during the reaction of superoxide reductase from Desulfoarculus baarsii with superoxide: Re-evaluation of the reaction mechanism

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• 作者：Florence Bonnot ; Chantal Hou&#xe9 ; e-Levin ; Vincent Favaudon ; Vincent Nivi&#xe8 ; re
• 关键词：Superoxide reductase ; Pulse radiolysis ; Reaction intermediates ; Photochemical processes ; Desulfoarculus baarsii
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2010
• 出版时间：April 2010
• 年：2010
• 卷：1804
• 期：4
• 页码：762-767
• 全文大小：404 K

文摘

Superoxide reductase SOR is an enzyme involved in superoxide detoxification in some microorganisms. Its active site consists of a non-heme ferrous center in an unusual [Fe(NHis)₄ (SCys)₁] square pyramidal pentacoordination that efficiently reduces superoxide into hydrogen peroxide. In previous works, the reaction mechanism of the SOR from Desulfoarculus baarsii enzyme, studied by pulse radiolysis, was shown to involve the formation of two reaction intermediates T1 and T2. However, the absorption spectrum of T2 was reported with an unusual sharp band at 625 nm, very different from that reported for other SORs. In this work, we show that the sharp band at 625 nm observed by pulse radiolysis reflects the presence of photochemical processes that occurs at the level of the transient species formed during the reaction of SOR with superoxide. These processes do not change the stoichiometry of the global reaction. These data highlight remarkable photochemical properties for these reaction intermediates, not previously suspected for iron-peroxide species formed in the SOR active site. We have reinvestigated the reaction mechanism of the SOR from D. baarsii by pulse radiolysis in the absence of these photochemical processes. The T1 and T2 intermediates now appear to have absorption spectra similar to those reported for the Archaeoglobus fulgidus SOR enzymes. Although for some enzymes of the family only one transient was reported, on the whole, the reaction mechanisms of the different SORs studied so far seem very similar, which is in agreement with the strong sequence and structure homologies of their active sites.