Electron transport chain cytochrome reductase

Electron Transport Chain Cytochrome b5 and NADH cytochrome b5 Reductase... 

In the third complex of the electron transport chain, reduced coenzyme Q (UQHg) passes its electrons to cytochrome c via a unique redox pathway known as the Q cycle. UQ cytochrome c reductase (UQ-cyt c reductase), as this complex is known, involves three different cytochromes and an Fe-S protein. In the cytochromes of these and similar complexes, the iron atom at the center of the porphyrin ring cycles between the reduced Fe (ferrous) and oxidized Fe (ferric) states. 

Boxes indicate electron-transport chain complexes, whereas ovals represent the electron transporters UQ, RQ and cytochrome c. The open boxes represent complexes involved in the classical aerobic respiratory chain, whereas grey boxes represent complexes involved in malate dismutation. The vertical bar represents a scale for the standard redox potentials in mV. Translocation of protons by the complexes is indicated by H+ +. Abbreviations Cl, Clll and CIV, complexes I, III and IV of the respiratory chain cyt c, cytochrome c FRD, fumarate reductase Fum, fumarate SDH, succinate dehydrogenase Succ, succinate RQ, rhodoquinone UQ, ubiquinone. 

The principal function of cyt. c is to form complexes through a defined interface with protein partners in our cells. This is most established for eukaryotic cytochrome c within the mitochondrial electron transport chain (ETC), a process required for carrying out the oxidative phosphorylation of ATP.4 Formation of a complex with cyt. c reductase (an electron-donor protein from complex III) and cyt. c oxidase (an electron-acceptor protein from complex IV) leads to the transfer of electrons between otherwise separated proteins. More recently cyt. c has been found to play a critical role in the process of apoptosis or programmed cell death This in turn has led to a resurgence of interest in all aspects of cyt. c research.5 Again protein-protein interactions have been shown be essential with mitochrondrial cyt. c binding to such proteins as APAF-1 to form the multi-protein species known as the apoptosome that is now thought to be a requirement for apoptosis.6,7... 

Fig. 6. Sites of inhibitory action of DCMU in photosynthetic electron transport chain. The abbreviations are as follows - Cyt f cytochrome f, Fd ferredoxin, Mn water-splitting complex (manganese-containing), P680 pigment complex of photosystem II, P700 pigment complex of photosystem I, PC plastocyanin, PQ plastquinone, Q quencher, Rd NADP reductase and X direct electron acceptor complex...

Fig. 5.2. Possible metabolic pathways in facultative anaerobic mitochondria. Shaded boxes show components of the electron-transport chain used during hypoxia, open boxes are components used during aerobiosis, and the hatched boxes (complex I and ATP-synthase) are components used under aerobic as well as anaerobic conditions. ASCT acetate succinate CoA-transferase, C cytochrome c, Cl, CIII and CIV complexes I, III and IV of the respiratory chain, CITR citrate, ECR enoyl-CoA reductase (such as present in Ascaris suum), ETF electron-transfer flavoprotein, ETF RQ OR electron-transfer flavoproteimrhodoquinone oxidoreductase, FRD fumarate reductase, FUM fumarate, MAE malate, OXAC oxaloacetate, PYR pyruvate, RQ rhodoquinone, SDH succinate dehydrogenase, SUCC succinate, Succ-CoA succinyl-CoA, TER trans-2-enoyl-CoA reductase (such as present in E. gracilis), UQ ubiquinone...

Fig. 5.3. The major components involved in mitochondrial NADH oxidation in facultative anaerobic mitochondria. In anaerobically functioning mitochondria, NADH is oxidized either by soluble enzymes (left) or by membrane-bound complexes of the electron-transport chain (middle). Under aerobic conditions, a classic respiratory chain is used to oxidize NADH (right). Proton translocation is indicated by H with arrows. Ovals represent the electron transporters RQ, UQ and cytochrome c (cyt. c), and electron transport is indicated by dashed arrows. The vertical bar represents a scale for the standard redox potentials in millivolts. Fum fumarate, NADH-DH NADH dehydrogenase, NADH-ECR soluble NADH enoyl-CoA reductase, RQH2 rhodoquinol, Succ succinate, UQH2 ubiquinol...

Figure 3. Diagram of a section through the cell wall of Acidithiobacillus ferrooxidans modified from Blake et al. (1992) showing the relationship between iron oxidation and pyrite dissolution. OM =outer membrane, P = periplasm, IM = inner or (cytoplasmic) membrane, cty = cytochrome, pmf = proton motive force. Passage of a proton (driven by proton motive force) into the cell catalyzes the conversion of ADP to ATP. Ferrous iron binds to a component of the electron transport chain, probably a cytochrome c, and is oxidized. The electrons are passed to a terminal reductase where they are combined with O2 and to form water, preventing acidification of the cytoplasm. Ferric iron can either oxidize pyrite (e.g. within the ore body) or form nanocrystalline iron oxyhydroxide minerals (often in surrounding groundwater or streams).

The answer is c. (Murray, pp 123-148. Scriver, pp 2367-2424. Sack, pp 159-175. Wilson, pp 287-317.) The electron transport chain shown contains three proton pumps linked by two mobile electron carriers. At each of these three sites (NADH-Q reductase, cytochrome reductase, and cytochrome oxidase) the transfer of electrons down the chain powers the pumping of protons across the inner mitochondrial membrane. The blockage of electron transfers by specific point inhibitors leads to a buildup of highly reduced carriers behind the block because of the inability to transfer electrons across the block. In the scheme shown, rotenone blocks step A, antimycin A blocks step B, and carbon monoxide (as well as cyanide and azide) blocks step E. Therefore a carbon monoxide inhibition leads to a highly reduced state of all of the carriers of the chain. Puromycin and chloramphenicol are inhibitors of protein synthesis and have no direct effect upon the electron transport chain. 

Electron transport chain Present in the mitochondrial membrane, this linear array of redox active electron carriers consists of NADH dehydrogenase, coenzyme Q, cytochrome c reductase, cytochrome c, and cytochrome oxidase as well as ancillary iron sulfur proteins. The electron carriers are arrayed in order of decreasing reduction potential such that the last carrier has the most positive reduction potential and transfers electrons to oxygen. 

The components of the electron transport chain have various cofactors. Complex I, NADH dehydrogenase, contains a flavin cofactor and iron sulfur centers, whereas complex ID, cytochrome reductase, contains cytochromes b and Cj. Complex IV, cytochrome oxidase, which transfers electrons to oxygen, contains copper ions as well as cytochromes a and a. The general structure of the cytochrome cofactors is shown in Figure 16-2. Each of the cytochromes has a heme cofactor but they vary slightly. The b-type cytochromes have protoporphyrin IX, which is identical to the heme in hemoglobin. The c-type cytochromes are covalently bound to cysteine residue 10 in the protein. The a-type... 

A FIGURE 8-15 Heme and iron-sulfur prosthetic groups in the respiratory (electron-transport) chain, (a) Heme portion of cytochromes /jl and fan. which are components of the C0QH2-cytochrome c reductase complex. The same porphyrin ring (yellow) is present in all hemes. The chemical substituents attached to the porphyrin ring differ in the other cytochromes in... 

Fig. 39. Proposed parallel electron transport chains feeding the different steps of nitrogen reduction in P. denitrificans when it respires with nitrate. Each intermediate reaction step has its own nitrogen compound reductase (or cytochrome oxidase. After references 406-408.

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