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• W2054166841 endingPage "1445" @default.
• W2054166841 startingPage "1444" @default.
• W2054166841 abstract "Ultrafast kinetic measurements of NO rebinding to horseradish peroxidase (HRP) are reported for the first time. The geminate kinetics are found to be exponential for all HRP samples studied. The ferric forms of HRP have NO geminate recombination time constants in the range of 15−30 ps, while the ferrous form has a time constant of ∼7 ps. The simple exponential NO geminate kinetics found for HRP demonstrate that heme relaxation is not the underlying source of the nonexponential NO rebinding in myoglobin (Mb). The NO ligand escape rates from HRP are also determined, and they are found to depend dramatically on the presence or absence of the competitive inhibitor benzohydroxamic acid (BHA). The kinetic results indicate that, in contrast to Mb, there is direct solvent access to the distal heme pocket of HRP." @default.
• W2054166841 created "2016-06-24" @default.
• W2054166841 creator A5049580087 @default.
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• W2054166841 date "2006-01-12" @default.
• W2054166841 modified "2023-10-14" @default.
• W2054166841 title "Dynamics of Nitric Oxide Rebinding and Escape in Horseradish Peroxidase" @default.
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• W2054166841 doi "https://doi.org/10.1021/ja057172m" @default.
• W2054166841 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2768277" @default.
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• W2054166841 hasPublicationYear "2006" @default.
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