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Koji Oohora Yuta Miyazaki Takashi Hayashi 《Angewandte Chemie (Weinheim an der Bergstrasse, Germany)》2019,131(39):13951-13955
Myoglobin reconstituted with Ni tetradehydrocorrin was investigated as a model of F430‐containing methyl‐coenzyme M reductase, which catalyzes anaerobic methane generation. The NiII tetradehydrocorrin complex has a NiII/NiI redox potential of ?0.34 V vs. SHE and EPR spectroscopy indicates the formation of a NiI species upon reduction by dithionite. This redox potential is approximately 0.31 V more positive than that of F430. The NiI tetradehydrocorrin moiety is bound to the apo‐form of myoglobin to yield the reconstituted protein. Methane gas is generated in the reaction of the model with methyl iodide in the presence of the reconstituted protein under reductive conditions, whereas the NiI complex itself does not produce methane gas. This is the first example of a protein‐based functional model of F430‐containing methyl‐coenzyme M reductase. 相似文献
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Suhee Bang Sora Park Yong‐Min Lee Seungwoo Hong Kyung‐Bin Cho Wonwoo Nam 《Angewandte Chemie (Weinheim an der Bergstrasse, Germany)》2014,126(30):7977-7981
One‐electron reduction of mononuclear nonheme iron(III) hydroperoxo (FeIII OOH) and iron(III) alkylperoxo (FeIII OOR) complexes by ferrocene (Fc) derivatives resulted in the formation of the corresponding iron(IV) oxo complexes. The conversion rates were dependent on the concentration and oxidation potentials of the electron donors, thus indicating that the reduction of the iron(III) (hydro/alkyl)peroxo complexes to their one‐electron reduced iron(II) (hydro/alkyl)peroxo species is the rate‐determining step, followed by the heterolytic O O bond cleavage of the putative iron(II) (hydro/alkyl)peroxo species to give the iron(IV) oxo complexes. Product analysis supported the heterolytic O O bond‐cleavage mechanism. The present results provide the first example showing the one‐electron reduction of iron(III) (hydro/alkyl)peroxo complexes and the heterolytic O O bond cleavage of iron(II) (hydro/alkyl)peroxo species to form iron(IV) oxo intermediates which occur in nonheme iron enzymatic and Fenton reactions. 相似文献
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