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Updated: Apr 5, 2026

Application of Genetically Encoded Fluorescent Nitric Oxide (NO•) Probes, the geNOps, for Real-time Imaging of NO• Signals in Single Cells
Published on: March 16, 2017
NO2(-)-mediated nitrosylation of ferrous microperoxidase-11
Paolo Ascenzi1, Diego Sbardella2, Marco Fiocchetti3
1Interdepartmental Laboratory for Electron Microscopy, Roma Tre University, I-00146 Roma, Italy; Institute of Protein Biochemistry, National Research Council, I-80131, Napoli, Italy.
Abstract:
Microperoxidase-11 (MP11) is an undecapeptide derived from horse heart cytochrome c (cyt c) and characterized by a covalently-linked solvent-exposed heme group. Here, kinetics of the NO2(-)-mediated nitrosylation of ferrous MP11 (MP11-Fe(II)) is reported. Data were obtained between pH6.4 and 8.2, at 20.0°C. The NO2(-)-mediated conversion of MP11-Fe(II) to MP11-Fe(II)-NO requires one proton; accordingly, values of the apparent second-order rate constant (kon) decrease by about two orders of magnitude from (2.9±0.3)×10(1)M(-1)s(-1) to (5.0±0.6)×10(-1)M(-1)s(-1) upon increasing pH from 6.4 to pH8.2. The slope of the linear fitting of Logkon versus pH is -1.00±0.06. Values of kon for the NO2(-)-mediated nitrosylation of MP11-Fe(II) are similar to those of penta-coordinated cardiolipin-bound horse heart cyt c, exceeding by about two orders of magnitude those of wild-type horse heart cyt c. Present results highlight the role of heme distal residues in modulating horse heart cyt c reactivity.
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