ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2014
Cardiolipin modulates allosterically the nitrite reductase activity of horse heart cytochrome c.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins.Biomolecules · 2023Review
- Nitrite Reductase Activity of Ferrous Nitrobindins: A Comparative Study.International journal of molecular sciences · 2023Article
- Nitrous Oxide Emissions from Paddies: Understanding the Role of Rice Plants.Plants (Basel, Switzerland) · 2020Review
- Potential Pathway of Nitrous Oxide Formation in Plants.Frontiers in plant science · 2020Review
- Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of CytochromeOxidative medicine and cellular longevity · 2020Review
- Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions.Computational and structural biotechnology journal · 2020Article
- Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their RegulationPhysiological reviews · 2019Review
- Cyanide binding to ferrous and ferric microperoxidase-11.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- The nitrite reductase activity of horse heart carboxymethylated-cytochrome c is modulated by cardiolipin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Upon cardiolipin (CL) liposomes binding, horse heart cytochrome c (cytc) changes its tertiary structure disrupting the heme-Fe-Met80 distal bond, reduces drastically the midpoint potential, binds CO and NO with high affinity, displays peroxidase activity, and facilitates peroxynitrite isomerization. Here, the effect of CL liposomes on the nitrite reductase activity of ferrous cytc (cytc-Fe(II)) is reported. In the absence of CL liposomes, hexa-coordinated cytc-Fe(II) displays a very low value of the apparent second-order rate constant for the NO2 (-)-mediated conversion of cytc-Fe(II) to cytc-Fe(II)-NO (k on = (7.3 ± 0.7) × 10(-2) M(-1) s(-1); at pH 7.4 and 20.0 °C). However, CL liposomes facilitate the NO2 (-)-mediated nitrosylation of cytc-Fe(II) in a dose-dependent manner inducing the penta-coordination of the heme-Fe(II) atom. The value of k on for the NO2 (-)-mediated conversion of CL-cytc-Fe(II) to CL-cytc-Fe(II)-NO is 2.6 ± 0.3 M(-1) s(-1) (at pH 7.4 and 20.0 °C). Values of the apparent dissociation equilibrium constant for CL liposomes binding to cytc-Fe(II) are (2.2 ± 0.2) × 10(-6) M, (1.8 ± 0.2) × 10(-6) M, and (1.4 ± 0.2) × 10(-6) M at pH 6.5, 7.4, and 8.1, respectively, and 20.0 °C. These results suggest that the NO2 (-)-mediated conversion of CL-cytc-Fe(II) to CL-cytc-Fe(II)-NO could play anti-apoptotic effects impairing lipid peroxidation and therefore the initiation of the cell death program by the release of pro-apoptotic factors (including cytc) in the cytoplasm.
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