Iron transitions during activation of allosteric heme proteins in cell signaling

Metallomics ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 868-893 ◽  
Author(s):  
Michel Négrerie
Keyword(s):  
Cell Signaling ◽  
Heme Proteins ◽  
Electrostatic Interactions ◽  
Redox State ◽  
Iron Coordination ◽  
Heme Distortion

Allosteric heme proteins can fulfill a very large number of different functions, thanks to the remarkable chemical versatility of the heme through the entire living kingdom. The involved heme properties include: changes of iron coordination and redox state, heme macrocycle electrostatic interactions and heme distortion.

scholarly journals Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of Cytochrome c and Cardiolipin

2020 ◽  
Vol 2020 ◽  
pp. 1-20 ◽  
Author(s):  
Antonio Díaz-Quintana ◽  
Gonzalo Pérez-Mejías ◽  
Alejandra Guerra-Castellano ◽  
Miguel A. De la Rosa ◽  
Irene Díaz-Moreno
Keyword(s):  
Lipid Membranes ◽  
Electrostatic Interactions ◽  
Current Knowledge ◽  
Reaction Pathway ◽  
Heme Iron ◽  
Amino Acid Residues ◽  
Experimental Conditions ◽  
Iron Coordination ◽  
The Stability ◽  
Key Aspects

Cardiolipin oxidation and degradation by different factors under severe cell stress serve as a trigger for genetically encoded cell death programs. In this context, the interplay between cardiolipin and another mitochondrial factor—cytochrome c—is a key process in the early stages of apoptosis, and it is a matter of intense research. Cytochrome c interacts with lipid membranes by electrostatic interactions, hydrogen bonds, and hydrophobic effects. Experimental conditions (including pH, lipid composition, and post-translational modifications) determine which specific amino acid residues are involved in the interaction and influence the heme iron coordination state. In fact, up to four binding sites (A, C, N, and L), driven by different interactions, have been reported. Nevertheless, key aspects of the mechanism for cardiolipin oxidation by the hemeprotein are well established. First, cytochrome c acts as a pseudoperoxidase, a process orchestrated by tyrosine residues which are crucial for peroxygenase activity and sensitivity towards oxidation caused by protein self-degradation. Second, flexibility of two weakest folding units of the hemeprotein correlates with its peroxidase activity and the stability of the iron coordination sphere. Third, the diversity of the mode of interaction parallels a broad diversity in the specific reaction pathway. Thus, current knowledge has already enabled the design of novel drugs designed to successfully inhibit cardiolipin oxidation.

Role of Heme Distortion on Oxygen Affinity in Heme Proteins: The Protoglobin Case

2010 ◽  
Vol 114 (25) ◽  
pp. 8536-8543 ◽  
Author(s):  
Damián E. Bikiel ◽  
Flavio Forti ◽  
Leonardo Boechi ◽  
Marco Nardini ◽  
F. Javier Luque ◽  
...  
Keyword(s):  
Heme Proteins ◽  
Oxygen Affinity ◽  
Heme Distortion

scholarly journals The Ascorbic Acid Redox State Controls Guard Cell Signaling and Stomatal Movement

2004 ◽  
Vol 16 (5) ◽  
pp. 1143-1162 ◽  
Author(s):  
Zhong Chen ◽  
Daniel R. Gallie
Keyword(s):  
Ascorbic Acid ◽  
Cell Signaling ◽  
Guard Cell ◽  
Redox State ◽  
Stomatal Movement

Template mediated crystal engineering

1994 ◽  
Vol 52 ◽  
pp. 480-481
Author(s):  
Brigid R. Heywood ◽  
S. Champ
Keyword(s):  
Crystal Engineering ◽  
Electrostatic Interactions ◽  
Alkyl Chain ◽  
Crystallographic Axis ◽  
Two Dimensional ◽  
Engineering Process ◽  
Solution Interface ◽  
Extensive Program ◽  
Geometric Homology ◽  
Long Alkyl Chain

Recent work on the crystallisation of inorganic crystals under compressed monomolecular surfactant films has shown that two dimensional templates can be used to promote the oriented nucleation of solids. When a suitable long alkyl chain surfactant is cast on the crystallisation media a monodispersied population of crystals forms exclusively at the monolayer/solution interface. Each crystal is aligned with a specific crystallographic axis perpendicular to the plane of the monolayer suggesting that nucleation is facilitated by recognition events between the nascent inorganic solid and the organic template.For example, monolayers of the long alkyl chain surfactant, stearic acid will promote the oriented nucleation of the calcium carbonate polymorph, calcite, on the (100) face, whereas compressed monolayers of n-eicosyl sulphate will induce calcite nucleation on the (001) face, (Figure 1 & 2). An extensive program of research has confirmed the general principle that molecular recognition events at the interface (including electrostatic interactions, geometric homology, stereochemical complementarity) can be used to promote the crystal engineering process.

O activation in cytochrome oxidase and in other heme proteins

1992 ◽  
Vol 1101 (2) ◽  
pp. 192-194
Author(s):  
G BABCOCK ◽  
C VAROTSIS ◽  
Y ZHANG
Keyword(s):  
Cytochrome Oxidase ◽  
Heme Proteins
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