St John 2012 Cell Tissue Res

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St John JC (2012) Transmission, inheritance and replication of mitochondrial DNA in mammals: implications for reproductive processes and infertility. Cell Tissue Res 349:795-808.

Β» PMID: 22696172

St John JC (2012) Cell Tissue Res

Abstract: The mitochondrial genome contributes key proteins to the electron-transfer chain, which through oxidative phosphorylation, generates the vast majority of cellular ATP. This maternally inherited genome is transmitted to subsequent generations through the oocyte. Its transmission, inheritance and replication are strictly regulated so that fully mature cells can be appropriately populated with mitochondrial DNA once they mature into adult cells. However, gametes do not always acquire the appropriate numbers of mitochondrial DNA copy; this often renders them inappropriate for successful fertilisation outcome. Furthermore, the number of assisted reproductive technologies that can overcome problems associated with infertility and that can provide enhanced genetic outcomes for the offspring is increasing. However, such techniques could also have a detrimental effect on offspring survival. If we are to introduce these technologies into in vitro fertilisation clinics and animal production, then we first need to validate their use carefully.


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Correction: FADH2 and Complex II

Ambiguity alert.png
FADH2 is shown as the substrate feeding electrons into Complex II (CII). This is wrong and requires correction - for details see Gnaiger (2024).
Gnaiger E (2024) Complex II ambiguities ― FADH2 in the electron transfer system. J Biol Chem 300:105470. - Β»Bioblast linkΒ«

Hydrogen ion ambiguities in the electron transfer system

Communicated by Gnaiger E (2023-10-08) last update 2023-11-10
Electron (e-) transfer linked to hydrogen ion (hydron; H+) transfer is a fundamental concept in the field of bioenergetics, critical for understanding redox-coupled energy transformations.
Ambiguity alert H+.png
However, the current literature contains inconsistencies regarding H+ formation on the negative side of bioenergetic membranes, such as the matrix side of the mitochondrial inner membrane, when NADH is oxidized during oxidative phosphorylation (OXPHOS). Ambiguities arise when examining the oxidation of NADH by respiratory Complex I or succinate by Complex II.
Ambiguity alert e-.png
Oxidation of NADH or succinate involves a two-electron transfer of 2{H++e-} to FMN or FAD, respectively. Figures indicating a single electron e- transferred from NADH or succinate lack accuracy.
Ambiguity alert NAD.png
The oxidized NAD+ is distinguished from NAD indicating nicotinamide adenine dinucleotide independent of oxidation state.
NADH + H+ β†’ NAD+ +2{H++e-} is the oxidation half-reaction in this H+-linked electron transfer represented as 2{H++e-} (Gnaiger 2023). Putative H+ formation shown as NADH β†’ NAD+ + H+ conflicts with chemiosmotic coupling stoichiometries between H+ translocation across the coupling membrane and electron transfer to oxygen. Ensuring clarity in this complex field is imperative to tackle the apparent ambiguity crisis and prevent confusion, particularly in light of the increasing number of interdisciplinary publications on bioenergetics concerning diagnostic and clinical applications of OXPHOS analysis.
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