Abstract
Cytochrome c oxidase is the terminal complex of eukaryotic oxidative phosphorylation in mitochondria. This process couples the reduction of electron carriers during metabolism to the reduction of molecular oxygen to water and translocation of protons from the internal mitochondrial matrix to the inter-membrane space. The electrochemical gradient formed is used to generate chemical energy in the form of adenosine triphosphate to power vital cellular processes. Cytochrome c oxidase and most oxidative phosphorylation complexes are the product of the nuclear and mitochondrial genomes. This poses a series of topological and temporal steps that must be completed to ensure efficient assembly of the functional enzyme. Many assembly factors have evolved to perform these steps for insertion of protein into the inner mitochondrial membrane, maturation of the polypeptide, incorporation of co-factors and prosthetic groups and to regulate this process. Much of the information about each of these assembly factors has been gleaned from use of the single cell eukaryote Saccharomyces cerevisiae and also mutations responsible for human disease. This review will focus on the assembly factors of cytochrome c oxidase to highlight some of the outstanding questions in the assembly of this vital enzyme complex.
Highlights
Energy generation is a fundamental process that supports all forms of life on earth
In eukaryotes a major portion of adenosine triphosphate (ATP) is generated through mitochondria, a double-membrane organelle derived from a symbiotic relationship at the origin of multicellular life [1]
FAD/FADH2 is reduced by succinate dehydrogenase of the citric acid cycle which acts as complex II of the electron transport chain (ETC)
Summary
Energy generation is a fundamental process that supports all forms of life on earth. The universal energy currency in life is adenosine triphosphate (ATP) which captures energy from bioenergetic and metabolic processes powered by substrate-level and oxidative phosphorylation. Mitochondria harbour a series of multi-subunit complexes that perform electron transfer and proton translocation from the internal mitochondrial matrix space to the inter-membrane space (IMS) through the inner mitochondrial (IMM). As oxidative phosphorylation (OXPHOS) is an evolutionarily conserved process in all eukaryotes much understanding of the assembly process can be gleaned from the study from all eukaryotic organisms where mitochondria exist This is true for single cell eukaryotes such as the budding yeast Saccharomyces cerevisiae and photosynthetic alga Chlamydomoas reinhardtii to multicellular higher eukaryotes such as human and mouse. The molecular details of the most studied mammalian organisms and yeast OXPHOS complex structure and assembly have very many similarities and some differences These differences are in the number of structural subunits forming complexes as well as the post-translational processing required for correct assembly. More homologues have been identified in higher eukaryotes demonstrating the conservation of the assembly of the complex as well as the enzymatic function [3]
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