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4-Ferredoxins

6 Ferredoxins. - Kostic and Popchapsky have reviewed the approaches used in their laboratory for stud3ring Cys4Fe2S2 ferredoxins and Ni(II)-contain-ing acireductone dioxygenase. They emphasize the utility of C-detected 2D [Pg.579]

Calzolai et al. have used and NMR to study the paramagnetic cluster environment of ferredoxin from the hyperthermophilic archaeon, Pyrococcus furiosus. They identified dipolar connectivities involving the strongly relaxed residues near the metal centers by a combination of Ti data, rapid pulsing and/or short delay/mixing time H WEFT spectra, NOESY, TOCSY, and HSQC maps. [Pg.580]

Sham et have used paramagnetically-induced relaxation enhancements as distance constraints for a solution molecular model of the ferredoxin of P. furiosus. Kostic et have used H Overhauser enhancements to compare the functional C-terminal domains of three vertebrate-type ferredoxins. [Pg.580]

Trivelli et and Ubbink have reviewed NMR studies of the interactions among proteins of the photosynthetic electron transfer chain. Mueller et report the NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase. [Pg.580]


Figure 8.39 Fourier transformed Fe extended X-ray absorption fine structure (EXAFS) and retransformation, after applying a 0.9-3.5 A filter window, of (a) a rubredoxin, (b) a plant ferredoxin and (c) a bacterial ferredoxin, whose structures are also shown. (Reproduced, with permission, Ifom Teo, B. K. and Joy, D. C. (Eds), EXAFS Spectroscopy, p. 15, Plenum, New York, 1981)... Figure 8.39 Fourier transformed Fe extended X-ray absorption fine structure (EXAFS) and retransformation, after applying a 0.9-3.5 A filter window, of (a) a rubredoxin, (b) a plant ferredoxin and (c) a bacterial ferredoxin, whose structures are also shown. (Reproduced, with permission, Ifom Teo, B. K. and Joy, D. C. (Eds), EXAFS Spectroscopy, p. 15, Plenum, New York, 1981)...
Iron Sulfur Compounds. Many molecular compounds (18—20) are known in which iron is tetrahedraHy coordinated by a combination of thiolate and sulfide donors. Of the 10 or more stmcturaHy characterized classes of Fe—S compounds, the four shown in Figure 1 are known to occur in proteins. The mononuclear iron site REPLACE occurs in the one-iron bacterial electron-transfer protein mbredoxin. The [2Fe—2S] (10) and [4Fe—4S] (12) cubane stmctures are found in the 2-, 4-, and 8-iron ferredoxins, which are also electron-transfer proteins. The [3Fe—4S] voided cubane stmcture (11) has been found in some ferredoxins and in the inactive form of aconitase, the enzyme which catalyzes the stereospecific hydration—rehydration of citrate to isocitrate in the Krebs cycle. In addition, enzymes are known that contain either other types of iron sulfur clusters or iron sulfur clusters that include other metals. Examples include nitrogenase, which reduces N2 to NH at a MoFe Sg homocitrate cluster carbon monoxide dehydrogenase, which assembles acetyl-coenzyme A (acetyl-CoA) at a FeNiS site and hydrogenases, which catalyze the reversible reduction of protons to hydrogen gas. [Pg.442]

A second example is that of an Ala-to-Cys mutation, which causes the fonnation of a rare SH S hydrogen bond between the cysteine and a redox site sulfur and a 50 mV decrease in redox potential (and vice versa) in the bacterial ferredoxins [73]. Here, the side chain contribution of the cysteine is significant however, a backbone shift can also contribute depending on whether the nearby residues allow it to happen. Site-specific mutants have confirmed the redox potential shift [76,77] and the side chain conformation of cysteine but not the backbone shift in the case with crystal structures of both the native and mutant species [78] the latter can be attributed to the specific sequence of the ferre-doxin studied [73]. [Pg.407]

Nonrepetitive but well-defined structures of this type form many important features of enzyme active sites. In some cases, a particular arrangement of coil structure providing a specific type of functional site recurs in several functionally related proteins. The peptide loop that binds iron-sulfur clusters in both ferredoxin and high potential iron protein is one example. Another is the central loop portion of the E—F hand structure that binds a calcium ion in several calcium-binding proteins, including calmodulin, carp parvalbumin, troponin C, and the intestinal calcium-binding protein. This loop, shown in Figure 6.26, connects two short a-helices. The calcium ion nestles into the pocket formed by this structure. [Pg.182]

The immediate electron acceptor for P700 is a special molecule of chlorophyll. This unique Chi a (Aq) rapidly passes the electron to a specialized quinone (Aj), which in turn passes the e to the first in a series of membrane-bound ferredoxins (Fd, Chapter 21). This Fd series ends with a soluble form of ferredoxin, Fd, which serves as the immediate electron donor to the fiavo-protein (Fp) that catalyzes NADP reduction, namely, ferredoxin NADP reductase. [Pg.722]

Figure 25.9 Some non-haem iron proteins (a) rubredoxin in which the single Fe is coordinated, almost tetra-hedrally, to 4 cysteine-sulfurs, (b) plant ferredoxin, [Fe2S2(S-Cys)4], (c) [Fe4S4(S-Cys)4] cube of bacterial ferredoxins. (This is in fact distorted, the Fe4 and S4 making up the two interpenetrating tetrahedra, of which the latter is larger than the former). Figure 25.9 Some non-haem iron proteins (a) rubredoxin in which the single Fe is coordinated, almost tetra-hedrally, to 4 cysteine-sulfurs, (b) plant ferredoxin, [Fe2S2(S-Cys)4], (c) [Fe4S4(S-Cys)4] cube of bacterial ferredoxins. (This is in fact distorted, the Fe4 and S4 making up the two interpenetrating tetrahedra, of which the latter is larger than the former).
The reductions are effected in nature by ferredoxin (p. 1102). This behaviour can be reproduced surprisingly well by simpler, model compounds. Some of the best known of these are obtained by the addition of axial groups to the square-planar complexes of Co with Schiff bases, or substituted glyoximes (giving cobaloximes) as illustrated in Fig. 26.7. The reduced Co species of these, along with vitamin... [Pg.1139]


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2-Iron ferredoxin models

2-Oxoacid:ferredoxin oxidoreductase Sulfolobus

2-Oxoacid:ferredoxin oxidoreductases

26- Hydroxylation ferredoxin

26- Hydroxylation ferredoxin reductase

7Fe ferredoxin

8-Fe Ferredoxins

Aldehyde Ferredoxin Oxidoreductase Family

Aldehyde: ferredoxin oxidoreductase Pyrococcus furiosus

Algal ferredoxin

Amino acid sequences ferredoxins

Azotobacter vinelandii ferredoxin

Bacterial ferredoxins

Bacterial ferredoxins molecular weight

Chloroplast ferredoxin

Chloroplast ferredoxins, biological

Clostridial ferredoxin

Clostridial ferredoxin isolation

Conformations ferredoxin

Enzymatic ferredoxins

Enzyme aldehyde ferredoxin oxidoreductase

Ferredoxin

Ferredoxin Fe

Ferredoxin II

Ferredoxin aldehyde oxidoreductase

Ferredoxin background, XII

Ferredoxin bacterial

Ferredoxin bound sulfite reduction

Ferredoxin chemical properties

Ferredoxin chemical properties, XII

Ferredoxin crystals, clostridium

Ferredoxin domain structure

Ferredoxin electrodes

Ferredoxin electron transfer kinetics

Ferredoxin from chloroplasts

Ferredoxin fusion protein with

Ferredoxin genes

Ferredoxin hydrogenase

Ferredoxin in methane bacteria

Ferredoxin in reductive biosynthesis

Ferredoxin isolation

Ferredoxin marismortui)

Ferredoxin mitochondrial 26-hydroxylation

Ferredoxin molecular weight

Ferredoxin oxidoreductase

Ferredoxin peptide model complexes

Ferredoxin physical properties, XII

Ferredoxin plant-type

Ferredoxin properties

Ferredoxin proteins

Ferredoxin reconstitution

Ferredoxin redox couples

Ferredoxin reducing substance

Ferredoxin reductase

Ferredoxin reduction potentials

Ferredoxin resonance Raman spectroscopy

Ferredoxin stability

Ferredoxin standard redox potential

Ferredoxin thermodynamics

Ferredoxin thermophile

Ferredoxin thioredoxin reductase

Ferredoxin, Sulfolobus

Ferredoxin, Sulfolobus purification

Ferredoxin, iron-sulfur anions

Ferredoxin, models

Ferredoxin, reactions

Ferredoxin-NAD oxidoreductase

Ferredoxin-NAD reductase

Ferredoxin-NADP

Ferredoxin-NADP oxidoreductase

Ferredoxin-NADP+ reductase

Ferredoxin-like fold

Ferredoxin-nitrate reductase

Ferredoxin-nitrite reductase

Ferredoxin-quinone reductase

Ferredoxin/thioredoxin system

Ferredoxine

Ferredoxins 2-iron

Ferredoxins Anabaena

Ferredoxins EXAFS

Ferredoxins Fe2S2

Ferredoxins Fe4S4

Ferredoxins Rieske

Ferredoxins Subject

Ferredoxins advantage over rubredoxins

Ferredoxins amino acid sequence comparisons

Ferredoxins containing zinc

Ferredoxins defined

Ferredoxins determination

Ferredoxins electronic properties

Ferredoxins evolution

Ferredoxins history

Ferredoxins interconversions

Ferredoxins iron ligands

Ferredoxins iron-sulfur center

Ferredoxins ligands

Ferredoxins magnetic properties

Ferredoxins photosynthetic reactions

Ferredoxins polypeptide fold and metal centers

Ferredoxins properties

Ferredoxins redox potentials

Ferredoxins spectroscopy

Ferredoxins structure

Ferredoxins structures, crystallographic

Ferredoxins substitutes

Ferredoxins types

Ferredoxins, molecular electronic

Generation of hydroxyl radicals by ferredoxin systems

Glutamate synthase ferredoxin dependent

Iron-sulfur ferredoxin

Iron-sulfur proteins ferredoxins

Iron-sulfur proteins pyruvate-ferredoxin oxidoreductase

Iron-sulphur clusters Ferredoxins

Mononuclear iron-sulfur clusters ferredoxins

Naphthalene Rieske ferredoxin

Nitrogen-fixing bacteria ferredoxins

Of 7Fe ferredoxin

Peptococcus aerogenes ferredoxin

Photosynthesis ferredoxin

Photosynthesis ferredoxin/thioredoxin system

Photosynthesis ferredoxins

Plant type ferredoxins

Plants, higher Ferredoxin

Proteins ferredoxins

Pyrococcus furiosus ferredoxin

Pyruvate ferredoxin reductase

Pyruvate-ferredoxin oxidoreductase

Pyruvate-ferredoxin oxidoreductase metronidazole

Pyruvate:ferredoxin oxidoreductase PFOR)

Redox potentials Ferredoxin, NADPH

Reduced Ferredoxin in Reductive Biosynthesis

Reduction-oxidation potentials Ferredoxin

Spinach ferredoxin

Spinach ferredoxin reduction potential

Sulfate-reducing bacteria ferredoxins

Thermotoga maritima ferredoxin

Three-dimensional structures ferredoxin

Two-iron ferredoxins

Zinc-containing ferredoxin

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