Ferredoxin, reactions

Examples of ferredoxin reactions can be observed in the scheme reproduced in Fig. 5.1. Some of these reactions such as the reduction of NAD to NADH by Hj,... 

The use of direct electrochemical methods (cyclic voltammetry Pig. 17) has enabled us to measure the thermodynamic parameters of isolated water-soluble fragments of the Rieske proteins of various bci complexes (Table XII)). (55, 92). The values determined for the standard reaction entropy, AS°, for both the mitochondrial and the bacterial Rieske fragments are similar to values obtained for water-soluble cytochromes they are more negative than values measured for other electron transfer proteins (93). Large negative values of AS° have been correlated with a less exposed metal site (93). However, this is opposite to what is observed in Rieske proteins, since the cluster appears to be less exposed in Rieske-type ferredoxins that show less negative values of AS° (see Section V,B). 

Cluster 1 is a conventional [4Fe-4S] cubane cluster bound near the N-terminus of the molecule as shown in Fig. 13. Within the cluster the Fe-S bonds range from 2.26 to 2.39 A. The cluster is linked to the protein by four cysteine residues with Fe-S distances ranging from 2.21 to 2.35 A, but the distribution of the cysteine residues along the polypeptide chain contrasts markedly with that found, for example, in the ferredoxins as indicated in Section II,B,4 [also see, for example, 41) and references therein]. In the Fepr protein all four cysteine residues (Cys 3, 6, 15, and 21) originate from the N-terminus of the molecule, and the fold of the polypeptide chain in this region is such that it wraps itself tightly around the cluster, yet keeps it near the surface of the molecule. In such a position the cluster is ideally placed to participate in one-electron transfer reactions with other molecules. 

The subunits of CODH/ACS have been isolated (see earlier discussion). The isolated a subunit contains one Ni and four Fe and has spectroscopic properties (186) similar to those of Cluster A, the active site of acetyl-CoA synthesis (212). Unfortunately, it has no ACS activity. Therefore, ACS activity may reside in the a subunit or it may require both the a and the fi subunits. If Clusters B and/or C of the B subunit are involved in acetyl-CoA synthesis, one possible role could be in electron transfer. Although acetyl-CoA synthesis and the CO/ exchange reactions do not involve net electron transfer, both of these reactions are stimulated by ferredoxin, indicating that internal electron transfer within CODH/ACS may be required during the reaction (121). Further studies with the isolated subunits and the reconstitu-... 

The 2[4Fe-4S] and [3Fe-4S][4Fe-4S] ferredoxins are components of virtually all eubacteria and archaebacteria (3). Several comprehensive reviews dealing with these small metalloproteins have appeared (3, 8-12), but only those participating directly in the photosynthetic light reactions will be addressed here. 

H)2-D3 is a weak agonist and must be modified by hydroxylation at position Cj for full biologic activity. This is accomplished in mitochondria of the renal proximal convoluted tubule by a three-component monooxygenase reaction that requires NADPFl, Mg, molecular oxygen, and at least three enzymes (1) a flavoprotein, renal ferredoxin reductase (2) an iron sulfur protein, renal ferredoxin and (3) cytochrome P450. This system produces l,25(OH)2-D3, which is the most potent namrally occurring metabolite of vitamin D. 

Scheumann, V., Schoch, S., and Rudiger, W., Chlorophyll A formation in the chlorophyll b reductase reaction requires reduced ferredoxin, J. Biol. Chem., 273, 35102, 1998. 

Details of the mechanism of naphthalene dioxygenase during a single turnover of the enzyme have been revealed, and conhrmed the separate roles of the dioxygenase and the ferredoxin electron transfer protein. This made it possible to propose a reaction cycle for the reaction (Wolfe et al. 2001). 

Figure 12.2a. Photosynthetic Z-scheme for green plants. Abbreviations not included in the text are PQ, plastiquinone Cyt bse, a form of cytochrome b absorbing at 564 nm FD, ferredoxin FP a flavoprotein. Long vertical arrows indicate steps arising from photoactivation of pigment reaction centers dashed arrows indicate uncertain pathways.0185...

Fe-S complexes have important functions in today s living systems, in enzymes such as the ferredoxins and oxidoreductases, as well as in electron transport proteins. It is striking that these redox reactions mainly involve elements and compounds such as CO, H2 and N2, which were probably also components of the primeval Earth s atmosphere. Thus, the assumption of an active involvement of Fe-S clusters in a (hypothetical) Fe-S world in processes which finally led to biogenesis appears completely reasonable We now have a background to the theory of the chemoau-totrophic origin of life . 

Studies of ferredoxin [152] and a photosynthetic reaction center [151] have analyzed further the protein s dielectric response to electron transfer, and the protein s role in reducing the reorganization free energy so as to accelerate electron transfer [152], Different force fields were compared, including a polarizable and a non-polarizable force field [151]. One very recent study considered the effect of point mutations on the redox potential of the protein azurin [56]. Structural relaxation along the simulated reaction pathway was analyzed in detail. Similar to the Cyt c study above, several slow relaxation channels were found, which limited the ability to obtain very precise free energy estimates. Only semiquantitative values were... 

The reaction-center proteins for Photosystems I and II are labeled I and II, respectively. Key Z, the watersplitting enzyme which contains Mn P680 and Qu the primary donor and acceptor species in the reaction-center protein of Photosystem II Qi and Qt, probably plastoquinone molecules PQ, 6-8 plastoquinone molecules that mediate electron and proton transfer across the membrane from outside to inside Fe-S (an iron-sulfur protein), cytochrome f, and PC (plastocyanin), electron carrier proteins between Photosystems II and I P700 and Au the primary donor and acceptor species of the Photosystem I reaction-center protein At, Fe-S a and FeSB, membrane-bound secondary acceptors which are probably Fe-S centers Fd, soluble ferredoxin Fe-S protein and fp, is the flavoprotein that functions as the enzyme that carries out the reduction of NADP+ to NADPH. 

Metalloproteins fall into three main structure categories depending on whether the active site consists of a single coordinated metal atom, a metal-porphyrin unit, or metal atoms in a cluster arrangement. In the context of electron-transfer metalloproteins, the blue Cu proteins, cytochromes, and ferre-doxins respectively are examples of these different structure types. Attention will be confined here mainly to a discussion of the reactivity of the blue Cu protein plastocyanin. Reactions of cytochrome c are also considered, with brief mention of the [2Fe-2S] ferredoxin, and high potential Fe/S protein [HIPIP]. 

A number of examples of limiting kinetics have been reported for reactions of [2Fe-2S] and 2[4Fe-4S] ferredoxins with inorganic complexes (11). Recent stopped-flow work has not however confirmed limiting kinetics for the reaction of azurin, ACu(I) +... 

There has been considerable effort in the last few years toward achieving an understanding of hydrogenase enzyme systems which have the ability to activate H2 for exchange with water, para-ortho conversion, and reduction reactions when coupled to an electron carrier E such as NAD+, cytochrome c3, or ferredoxins (7, p. 396 470-473). Reaction (81) can be catalyzed in either direction ... 

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