المؤلفون: Xuyan Ru (1883452), Brian R. Crane (281294), Peng Zhang (2071), David N. Beratan (1314567)

مصطلحات موضوعية: Biophysics, Biochemistry, Molecular Biology, Chemical Sciences not elsewhere classified, Aromatics Fail, Experimental studies, tunneling distance, Cc heme, tyrosine vs tryptophan oxidation ac., charge recombination, Trp 191, Small molecules, charge recombination rates, Tryptophan 191, study interprotein electron transfer, redox-active aniline derivatives, cytochrome c peroxidase, Support Hole Hopping, CcP, water splitting, W 191G species, binding pocket, electron transport, W 191G cavity, Trp site, W 191F, guest molecule, W 191Y, oxidative damage protection, ET kinetics

Relation: https://figshare.com/articles/journal_contribution/Why_Do_Most_Aromatics_Fail_to_Support_Hole_Hopping_in_the_Cytochrome_i_c_i_Peroxidase_Cytochrome_i_c_i_Complex_/14932284

الاتاحة: https://doi.org/10.1021/acs.jpcb.1c05064.s001

المؤلفون: Mary Ortmayer (8437401), Florence J. Hardy (10801578), Matthew G. Quesne (1298382), Karl Fisher (1740823), Colin Levy (2334499), Derren J. Heyes (110340), C. Richard A. Catlow (7163117), Sam P. de Visser (7860788), Stephen E. J. Rigby (8437413), Sam Hay (1982488), Anthony P. Green (1874023)

مصطلحات موضوعية: Biophysics, Biochemistry, Genetics, Evolutionary Biology, Computational Biology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, code, porphyrin π- cation, site features, C c P W 191F compound, site Trp 51, reactivity manifests, Active Site Hydrogen Bond Controlli., Trp 51 tunes, Trp 191, noncanonical substitutions, ferryl heme states, metal-oxo coordination environments., activity increase, oxidative transformations, cytochrome c peroxidase, substrate binding site, metal-oxo structure, ferryl heme structure, C c P W 191F compound II, phenolic substrates, redox partner cyt c, function, Heme Peroxidase Nature

Relation: https://figshare.com/articles/journal_contribution/A_Noncanonical_Tryptophan_Analogue_Reveals_an_Active_Site_Hydrogen_Bond_Controlling_Ferryl_Reactivity_in_a_Heme_Peroxidase/14595822

الاتاحة: https://doi.org/10.1021/jacsau.1c00145.s001