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10.1021/acs.biochem.7b00432 http://scihub22266oqcxt.onion/10.1021/acs.biochem.7b00432 C5518273!5518273!28689401     free     free     free       Biochemistry 2017 ; 56 (28): 3531-8 Nephropedia Template TP {{tp|p=28689401|t=2017. Hole Hopping through Tryptophan in Cytochrome P450 |pdf=|usr=}}{{28689401}} gab.com Text Hole Hopping through Tryptophan in Cytochrome P450 JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=28689401 #FOAvip Electron-transfer kinetics have been measured in four conjugates of cytochrome P450 with surface-bound Ru-photosensitizers. The conjugates are constructed with enzymes from Bacillus megaterium (CYP102A1) and Sulfolobus acidocaldarius (CYP119). A W96 residue lies in the path between Ru and the heme in CYP102A1, whereas H76 is present at the analogous location in CYP119. Two additional conjugates have been prepared with (CYP102A1)W96H and (CYP119)H76W mutant enzymes. Heme oxidation by photochemically generated Ru3+ leads to P450 compound II formation when a tryptophan residue is in the path between Ru and the heme; no heme oxidation is observed when histidine occupies this position. The data indicate that heme oxidation proceeds via two-step tunneling through a tryptophan radical intermediate. In contrast, heme reduction by photochemically generated Ru+ proceeds in a single electron tunneling step with closely similar rate constants for all four conjugates. Twit Text FOAVip Hole Hopping through Tryptophan in Cytochrome P450 ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=28689401 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28689401 #FOAvip English Wikipedia <ref>{{Cite pmid|28689401}}</ref> Hole Hopping through Tryptophan in Cytochrome P450 #MMPMID28689401 Ener M; Gray HB; Winkler JR Biochemistry 2017[Jul]; 56 (28): 3531-8 PMID28689401show ga Electron-transfer kinetics have been measured in four conjugates of cytochrome P450 with surface-bound Ru-photosensitizers. The conjugates are constructed with enzymes from Bacillus megaterium (CYP102A1) and Sulfolobus acidocaldarius (CYP119). A W96 residue lies in the path between Ru and the heme in CYP102A1, whereas H76 is present at the analogous location in CYP119. Two additional conjugates have been prepared with (CYP102A1)W96H and (CYP119)H76W mutant enzymes. Heme oxidation by photochemically generated Ru3+ leads to P450 compound II formation when a tryptophan residue is in the path between Ru and the heme; no heme oxidation is observed when histidine occupies this position. The data indicate that heme oxidation proceeds via two-step tunneling through a tryptophan radical intermediate. In contrast, heme reduction by photochemically generated Ru+ proceeds in a single electron tunneling step with closely similar rate constants for all four conjugates. äHole Hopping through Tryptophan in Cytochrome P450 (epmc).pdf DeepDyve Pubget Overpricing