Homolytic cleavage of both heme-bound hydrogen peroxide and hydrogen sulfide leads to the formation of sulfheme
HD Arbelo-Lopez, NA Simakov, JC Smith… - The Journal of …, 2016 - ACS Publications
Many heme-containing proteins with a histidine in the distal E7 (HisE7) position can form
sulfheme in the presence of hydrogen sulfide (H2S) and a reactive oxygen species such as
hydrogen peroxide. For reasons unknown, sulfheme derivatives are formed specifically on
solvent-excluded heme pyrrole B. Sulfhemes severely decrease the oxygen-binding affinity
in hemoglobin (Hb) and myoglobin (Mb). Here, use of hybrid quantum mechanical/molecular
mechanical methods has permitted characterization of the entire process of sulfheme …
sulfheme in the presence of hydrogen sulfide (H2S) and a reactive oxygen species such as
hydrogen peroxide. For reasons unknown, sulfheme derivatives are formed specifically on
solvent-excluded heme pyrrole B. Sulfhemes severely decrease the oxygen-binding affinity
in hemoglobin (Hb) and myoglobin (Mb). Here, use of hybrid quantum mechanical/molecular
mechanical methods has permitted characterization of the entire process of sulfheme …
[引用][C] Homolytic Cleavage of Both Heme-Bound Hydrogen Peroxide and Hydrogen Sulfide Leads to the Formation of Sulfheme
LG Juan, W Troy - 2016
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