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  Members of the electron transport chain

Members of the electron transport chain:

The electron transport chain is started through the reaction of an organic metabolite (intermediate in metabolic reactions) along with the coenzyme NAD+ (nicotinamide adenine dinucleotide is a coenzyme consisting of the B-vitamin, nicotinamide). This is an oxidation reaction in which 2 hydrogen atoms (or 2 hydrogen ions and 2 electrons) are separated from the organic metabolite. (The organic metabolites are generally from the citric acid cycle and the oxidation of fatty acids—details in subsequent pages). The reaction can be presented simply where M = any metabolite.

MH2 + NAD+ → NADH + H+ M: + energy

Complex I:

NADH dehydrogenase as well called NADH coenzyme Q reductase situated in the inner mitochondrial membrane and as well contains non heme iron atoms. These dehydrogenase enzymes does not act in response with oxygen in place of an electron carrier is interposed among the metabolite and next member in the chain. These enzymes contain a protein part and a non protein part that is a coenzyme. The co enzyme NAD+ or NADP+ are used as the prime carriers of hydrogen.

Complex II:

Coenzyme Q (here Q stands for Quinone) or cytochrome c reductase is a Ubiquinone. It is within the inner membrane in the free form or protein bound form. Coenzyme Q takes place the position among the cytochrome and metalloflavoproteins in the chain. At the point of coenzyme the H+ ion detach and go into solution, leaving the electrons to the cytochromes.

Complex III:

Cytochrome coxidase. Cytochromes are extremely identical to the structure of myoglobin/hemoglobin. The important feature is the heme structure comprising the iron (Fe) ions, basically in the +3 state and changed to the +2 state through the addition of an electron. Cytochrome molecules accept just only the electron from every hydrogen, not the complete atom. The various types of cytochromes hold electrons at slightly dissimilar energy levels. Electrons are passed together from one cytochrome to the next in the chain, losing energy as they go. At last, the last cytochrome in the chain, cytochrome a, passes 2 electrons to molecular oxygen. These cytochromes are proteins which carry a prosthetic group that has an embedded metal atom. The protein ‘steals’ the capability of the metal atom to accept and release electrons.

Complex IV :
ATP synthase, also termed as the F0 F1 particle comprises two components F0 and F1 (F–points out the factor). F1 protruding in matrix from the inner membrane and F0 embedded and expand beyond the inner membrane. The protruding F1 is necessary for the energy coupling to ATP molecule. Thorough removal of this component (experimentally) leads to impairment in ATP production while the intact respiratory chain is available.

 

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