Electron transport sequence

These findings lead to (he conclusion that the reduction of MHb by its reductase requires a natural cofactor, which is abolished during the purification procedure and can be replaced by methylene blue (G5, H22, H23, K8, K14). Since methylene blue and the other effective dyes are redox intermediates, it is obvious that the postulated cofactor interacts in the electron transport sequence of the MHbR reaction (H23). This is confirmed by the finding that oxygen and cytochrome c serve as well as terminal electron acceptor as does MHb (H22, H23, K14). Nevertheless, it had been possible to separate a cytochrome c reductase from MHbR in yeast extracts (A6). 

The electron transport chain is vital to aerobic organisms. Interference with its action may be life threatening. Thus, cyanide and carbon monoxide bind to haem groups and inhibit the action of the enzyme cytochrome c oxidase, a protein complex that is effectively responsible for the terminal part of the electron transport sequence and the reduction of oxygen to water. 

The development by Chance of a dual wavelength spectrophotometer permitted easy observation of the state of oxidation or reduction of a given carrier within mitochondria.60 This technique, together with the study of specific inhibitors (some of which are indicated in Fig. 18-5 and Table 18-4), allowed some electron transport sequences to be assigned. For example, blockage with rotenone and amytal prevented reduction of the cytochrome system by NADH but allowed reduction by succinate and by other substrates having their own flavoprotein components in the chain. Artificial electron acceptors, some of which are shown in Table 18-5,... 

Figure 22.16 Reductive electron transport sequences in the action of rNDP reductase. 

There are three proteins required for the formation of unsaturated fatty acids from precursor saturated acids by the microsomal electron-transport chain. They are NADH-cytochrome reductase, cytochrome 5, and acyl-CoA desaturase. The reaction sequence (Fig. lA) requires molecular oxygen as a proton acceptor, and electrons from NADH. The electron-transport sequence commences with the reductase, passes through cytochrome b, and terminates with the cyanide-sensitive factor, acyl-CoA desaturase (Enoch et al., 1976). Both cytochrome b reductase and cytochrome b are amphipathic proteins in which the redox center is located at the hydrophilic end while the hydrophobic portion binds to lipid moieties (DePierre and Ernster, 1977). Several studies have demonstrated the ability of cytochrome b and cytochrome b reductase to undergo lateral diffusion both in microsomes and in liposomes during the course of electron transfer (Hackenbrock, 1976). 

Traditionally, the electron and proton transport pathways of photosynthetic membranes (33) have been represented as a "Z" rotated 90° to the left with noncycHc electron flow from left to right and PSII on the left-most and PSI on the right-most vertical in that orientation (25,34). Other orientations and more complex graphical representations have been used to depict electron transport (29) or the sequence and redox midpoint potentials of the electron carriers. As elucidation of photosynthetic membrane architecture and electron pathways has progressed, PSI has come to be placed on the left as the "Z" convention is being abandoned. Figure 1 describes the orientation in the thylakoid membrane of the components of PSI and PSII with noncycHc electron flow from right to left. 

The electron transport protein, cytochrome c, found in the mitochondria of all eukaryotic organisms, provides the best-studied example of homology. The polypeptide chain of cytochrome c from most species contains slightly more than 100 amino acids and has a molecular weight of about 12.5 kD. Amino acid sequencing of cytochrome c from more than 40 different species has revealed that there are 28 positions in the polypeptide chain where the same amino acid residues are always found (Figure 5.27). These invariant residues apparently serve roles crucial to the biological function of this protein, and thus substitutions of other amino acids at these positions cannot be tolerated. 

Although electrons move from more negative to more positive reduction potentials in the electron transport chain, it should be emphasized that the electron carriers do not operate in a simple linear sequence. This will become evident when the individual components of the electron transport chain are discussed in the following paragraphs. 

P. Mitchell (Nobel Prize for Chemistry, 1978) explained these facts by his chemiosmotic theory. This theory is based on the ordering of successive oxidation processes into reaction sequences called loops. Each loop consists of two basic processes, one of which is oriented in the direction away from the matrix surface of the internal membrane into the intracristal space and connected with the transfer of electrons together with protons. The second process is oriented in the opposite direction and is connected with the transfer of electrons alone. Figure 6.27 depicts the first Mitchell loop, whose first step involves reduction of NAD+ (the oxidized form of nicotinamide adenosine dinucleotide) by the carbonaceous substrate, SH2. In this process, two electrons and two protons are transferred from the matrix space. The protons are accumulated in the intracristal space, while electrons are transferred in the opposite direction by the reduction of the oxidized form of the Fe-S protein. This reduces a further component of the electron transport chain on the matrix side of the membrane and the process is repeated. The final process is the reduction of molecular oxygen with the reduced form of cytochrome oxidase. It would appear that this reaction sequence includes not only loops but also a proton pump, i.e. an enzymatic system that can employ the energy of the redox step in the electron transfer chain for translocation of protons from the matrix space into the intracristal space. 

D. S. German, R. P. Levine (1965) Cytochrome / and plastocyanin their sequence inthephotosynthetic electron transport chain of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA, 54 1665-1669... 

In order to relate structure and function at a more direct level, it is necessary to focus on systems which have better characterized structure than the complex membrane bound proteins like cyt c oxidase. One particularly useful paradigm in this context is the cytochrome c-cytochrome c peroxidase couple [18]. Cep is not involved in electron transport, per se its apparent function [19] is detoxification of hydrogen peroxide via the sequence H2O2 -I- cep Fe(III) -> H2O -I- cep Fe(IV) O (protein) compound ES ... 

The first cytochrome to be recognised as a component of the photosynthetic electron transport chain was cytochrome f [142]. The properties of cytochrome f have been reviewed [143,144], and amino-acid sequence information is available for pea, spinach, wheat and tobacco [145]. The axial ligand to the heme-Fe... 

Ered Sanger, a double Nobel Prize winner, sequenced the human mitochondrial genome back in 1981. This genome codes for 13 proteins and the mitochondrion possesses the genetic machinery needed to synthesize them. Thus, the mitochondria are a secondary site for protein synthesis in eukaryotic cells. It turns out that the 13 proteins coded for by the mitochondrial genome and synthesized in the mitochondria are critically important parts of the complexes of the electron transport chain, the site of ATP synthesis. The nuclear DNA codes for the remainder of the mitochondrial proteins and these are synthesized on ribosomes, and subsequently transported to the mitochondria. 

Reaction of 232 with 4-substituted l,3-oxazol-5(4/7)-one 247 led to diacylhydrazines 248 or to imidazole derivatives 249 depending on the reaction temperature (Scheme 24). l,2,4-Triazole-3-thione 250 was obtained by a two-step sequence from 232 with phenyl isothiocyanate and subsequent base-catalyzed cyclization of thiosemicarbazide 251. The effects of hydrazones 241-246 on inhibition of photosynthetic electron transport in spinach chloroplasts and chlorophyll content in the antialgal suspensions of Chlorella vulgaris were investigated <2005CEC622>. 

S-L-x(i i5)-R-(N/F/xF) or M-L-R-(S/N)-F, picked out 138 sequences with 67% showing similarity to known proteins involved in metabolic pathways, electron transport, protein import, protein folding and oxygen scavenging pathways (Carlton et al. 2007). There are undoubtedly variations on these consensus, as have been found during proteomic studies (our unpublished data). 

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