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Dynamics of nitric oxide rebinding and escape in horseradish peroxidase.
J Am Chem Soc. 2006 Feb 8;128(5):1444-5. doi: 10.1021/ja057172m.
2
Investigations of ferric heme cyanide photodissociation in myoglobin and horseradish peroxidase.
J Phys Chem B. 2013 Apr 18;117(15):4042-9. doi: 10.1021/jp401224f. Epub 2013 Apr 3.
3
Temperature-dependent studies of NO recombination to heme and heme proteins.
J Am Chem Soc. 2005 Dec 7;127(48):16921-34. doi: 10.1021/ja054249y.
4
Photoexcitation dynamics of NO-bound ferric myoglobin investigated by femtosecond vibrational spectroscopy.
J Phys Chem B. 2013 Mar 14;117(10):2850-63. doi: 10.1021/jp400055d. Epub 2013 Mar 4.
6
Ultrafast dynamics of diatomic ligand binding to nitrophorin 4.
J Am Chem Soc. 2010 Mar 3;132(8):2811-20. doi: 10.1021/ja910005b.

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Are Protein Cavities and Pockets Commonly Used by Redox Active Signalling Molecules?
Plants (Basel). 2023 Jul 9;12(14):2594. doi: 10.3390/plants12142594.
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The interplay between mitochondrial reactive oxygen species formation and the coenzyme Q reduction level.
Redox Biol. 2018 Sep;18:256-265. doi: 10.1016/j.redox.2018.07.018. Epub 2018 Jul 23.
3
Solvent Composition Drives the Rebinding Kinetics of Nitric Oxide to Microperoxidase.
Sci Rep. 2018 Mar 27;8(1):5281. doi: 10.1038/s41598-018-22944-z.
4
Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site.
Chem Sci. 2015 Jan 1;6(1):505-516. doi: 10.1039/c4sc02752c. Epub 2014 Oct 22.
7
Ultrafast dynamics of diatomic ligand binding to nitrophorin 4.
J Am Chem Soc. 2010 Mar 3;132(8):2811-20. doi: 10.1021/ja910005b.
8
Measurements of heme relaxation and ligand recombination in strong magnetic fields.
J Phys Chem B. 2009 Aug 6;113(31):10923-33. doi: 10.1021/jp9031805.
9
Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy.
Biochemistry. 2008 May 6;47(18):5156-67. doi: 10.1021/bi7025485. Epub 2008 Apr 12.
10
Coherence spectroscopy investigations of the low-frequency vibrations of heme: effects of protein-specific perturbations.
J Am Chem Soc. 2008 Apr 16;130(15):5231-44. doi: 10.1021/ja7104027. Epub 2008 Mar 20.

本文引用的文献

1
Temperature-dependent studies of NO recombination to heme and heme proteins.
J Am Chem Soc. 2005 Dec 7;127(48):16921-34. doi: 10.1021/ja054249y.
3
Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO.
Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11704-9. doi: 10.1073/pnas.0504932102. Epub 2005 Aug 5.
4
A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic model.
Biochim Biophys Acta. 2005 Jun 1;1749(2):234-51. doi: 10.1016/j.bbapap.2005.04.002. Epub 2005 Apr 25.
6
Human myoglobin recognition of oxygen: dynamics of the energy landscape.
Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):18000-5. doi: 10.1073/pnas.0408379102. Epub 2004 Dec 15.
7
Horseradish peroxidase: a modern view of a classic enzyme.
Phytochemistry. 2004 Feb;65(3):249-59. doi: 10.1016/j.phytochem.2003.10.022.
8
Competition with xenon elicits ligand migration and escape pathways in myoglobin.
Biophys J. 2004 Jan;86(1 Pt 1):435-47. doi: 10.1016/S0006-3495(04)74120-X.
9
Accessibility of oxygen with respect to the heme pocket in horseradish peroxidase.
Proteins. 2003 Nov 15;53(3):656-66. doi: 10.1002/prot.10475.
10
Water penetration and binding to ferric myoglobin.
Biochemistry. 2001 May 15;40(19):5728-37. doi: 10.1021/bi010067e.

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