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Hemerythrin iron oxidation

A suitable model for the oxygen carrier protein hemerythrin is [Fe2(Et-HPTB)(OBz)](BF4)2 (Et-HPTB = AWAT,iV -tetrakis[(N-ethyl-2-benzimidazolyl)methyl]-2-hydroxy-l,3-diaminopropane, OBz = benzoate). It can mimic the formation of a binuclear peroxo iron complex in the natural system (101). The measured value of -12.8 cm3 mol1 for the activation volume of the oxidation reaction together with the negative value of the activation entropy confirm the highly structured nature of the transition state. [Pg.24]

Figure 1. Comparison of the coordination spheres of the dinuclear iron sites in oxidized hemerythrin (Hr), ribonucleotide reductase (RNR), uteroferrin (Uf), and methane monooxygenase (MMO). Figure 1. Comparison of the coordination spheres of the dinuclear iron sites in oxidized hemerythrin (Hr), ribonucleotide reductase (RNR), uteroferrin (Uf), and methane monooxygenase (MMO).
The metal clusters are not the only similarity in the diiron-oxygen protein group. Another common denominator is that all can react with dioxygen, albeit in different states of oxidation. RNR-R2 (30) and MMOH (31) proteins have in common that both cleave an oxygen-oxygen bond, with the iron cluster as an active participant. Hemerythrin is different from these others with five histidines (1-7) in the cluster... [Pg.360]


See other pages where Hemerythrin iron oxidation is mentioned: [Pg.173]    [Pg.442]    [Pg.424]    [Pg.84]    [Pg.268]    [Pg.168]    [Pg.278]    [Pg.459]    [Pg.165]    [Pg.421]    [Pg.137]    [Pg.139]    [Pg.466]    [Pg.862]    [Pg.887]    [Pg.315]    [Pg.683]    [Pg.690]    [Pg.442]    [Pg.44]    [Pg.92]    [Pg.254]    [Pg.1957]    [Pg.2239]    [Pg.3475]    [Pg.6396]    [Pg.366]    [Pg.370]    [Pg.466]    [Pg.862]    [Pg.683]    [Pg.690]    [Pg.455]    [Pg.132]    [Pg.1061]    [Pg.377]    [Pg.138]    [Pg.171]    [Pg.175]    [Pg.118]    [Pg.908]    [Pg.200]    [Pg.26]    [Pg.166]    [Pg.253]    [Pg.1956]    [Pg.2238]   
See also in sourсe #XX -- [ Pg.240 ]




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