Pyrococcus furiosus ferredoxin

Zhang, J.D., Christensen, H.E.M., Ooi, B.L and Ulstrup, J. (2004) In situ STM imaging and direct electrochemistry of Pyrococcus furiosus ferredoxin assembled on thiolate-modified Au(lll) surfaces. Langmuir, 20,10200-10207. 

Robust voltammetry and in situ STM to molecular resolution have been achieved when the Au(lll)-electrode surfaces are modified by linker molecules, Fig. 8-10, prior to protein adsorption. Comprehensive voltammetric data are available for horse heart cyt and P. aeruginosa The latter protein, which we address in the next Section, has in a sense emerged as a paradigm for nanoscale bioelectrochemistry. We address first briefly two other proteins, viz. the electron transfer iron-sulfur protein Pyrococcus furiosus ferredoxin and the redox metalloenz5mie Achromobacter xylosoxidans copper nitrite reductase. 

R.E. Duderstadt, et al.. Effects of mutations in aspartate 14 on the spectroscopic properties of the [FejSJ" clusters in Pyrococcus furiosus ferredoxin. Biochemistry 1999, 38, 10585-10593. 

Mukund S, MWW Adams (1991) The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. J Biol Chem 266 14208-14216. 

Mukund S, MWW Adams (1995) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 270 8389-8392. 

Roy R, S Mukund, GJ Schut, DM Dunn, R Weiss, MWW Adams (1999) Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus the third of a putative five-member tungstoenzyme family. J Bacteriol 181 1171-1180. 

Ferredoxin rednctases in Pyrococcus furiosus inclnding aldehyde ferredoxin reductase, glyceraldehyde-3-phosphate ferredoxin oxidorednctase, and formaldehyde ferredoxin reductase (Roy et al. 1999). 

Hasan MN, Kwakemaak C, Sloof WG, Hagen WR, Heering HA. 2006. Pyrococcus furiosus 4Fe-ferredoxin, chemisorbed on gold, exhibits gated reduction and ionic strength dependent dimerization. J Biol Inorg Chem 11 651-662. 

Sequence comparisons may also suggest new ligands. Recently, the complete amino acid sequence for a ferredoxin from the thermophilic organism Pyrococcus furiosus was determined (Eccleston et al., 1991). All... 

Pyrimidinethione complexes, osmium, 37 296 Pyriminethionate, as bridging ligands in platinum dimers, 40 202-205 Pyrochlores, 17 108 Pyrococcus furiosus, 38 344-383 aldehyde ferredoxin oxidoreductase, 38 374-381... 

The aldehyde ferredoxin oxidoreductase from the hyperthermophile Pyrococcus furiosus was the first molybdopterin-dependent enzyme for which a three-dimensional structure became available.683,684 The tungstoenzyme resembles that of the related molybdo-enzyme (Fig. 16-31). A similar ferredoxin-dependent enzyme reduces glyceraldehyde-3-phosphate.685 Another member of the tungstoenzyme aldehyde oxidoreductase family is carboxylic acid reductase, an enzyme found in certain acetogenic clostridia. It is able to use reduced ferredoxin to convert unactivated carboxylic acids into aldehydes, even though E° for the acetaldehyde/acetate couple is -0.58 V.686... 

The crystal structure of aldehyde ferredoxin oxidoreductase (AOR) from the hyperthermophile Pyrococcus furiosus was the first of any molybdenum or tungsten enzyme (excepting nitrogenase) (42). The AOR was adopted as the parent name for the family of tungsten enzymes. The structure of formaldehyde ferredoxin oxidoreductase (FOR) has recently been solved (44). 

The conversion of pyruvate to acetyl-CoA is catalysed by pyruvate oxidoreductase in the archaebacteria. The enzyme has been detected and characterised in Halobacterium halobium[i, 2i2 Tp. acidophilum, S. acidocaldarius and Desulfurococcus mobilis[i i], Pyrococcus furiosus [34] and in Methanobacterium thermoautotrophicum [35]. In the halophiles and thermophiles, ferredoxin serves as electron acceptor, whereas the methanogens use the deazaflavin derivative F420. 

Fig. 14. Proposed pathway of maltose and of pyruvate fermentation to acetate, H2 and CO2 in Pyrococcus furiosus. Fdox, oxidized ferredoxin Fdred, reduced ferredoxin CoA, coenzymeA. Numbers in circles refer to enzymes involved (1) Q-glucosidase [296] (2) glucoserferredoxin oxidoreductase (3) gluconate dehydratase (this enzyme has not been detected so far in Pyrococcus furiosus) (4) 2-keto-3-deoxygluconate aldolase (5) glyceraldehyde ferredoxin oxidoreductase (6) glycerate kinase (2-phosphoglycerate forming) (7) enolase (8) pyruvate kinase (9) pyruvateiferredoxin oxidoreductase (10) ADP-forming acetyl-CoA synthetase (11)...

Telser, J., R. Davydov, C.-H. Kim, M.W.W. Adams, and B.M. Hoffman (1999). Investigation of the unusual electronic structure of Pyrococcus furiosus 4Fe ferredoxin by EPR spectroscopy of protein reduced at ambient and cryogenic temperatures. Inorg. Chem. 38, 3550-3553. 

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. 

Ma, K., Hutchins, A., Sung, S.J., and Adams, M.W. (1997) Pyruvate ferredoxin oxidoreductase from the hyper-thermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. Proc. Nad. Acad. Sci. U.S.A., 94 (18), 9608-9613. 

Hopkins, R.C., Sun, J., Jenney, F.E., Chandrayan, S.K., McTernan, P.M., and Adams, M.W.W. (2011) Homologous expression of a subcomplex of Pyrococcus furiosus hydrogenase that interacts with pyruvate ferredoxin oxidoreductase. PLoS One, 6, e26569. 

Mitra D, Pehnenschikov V et al (2011) Dynamics of the [4Fe-4S] cluster in pyrococcus furiosus D14C ferredoxin via nuclear resonance vibrational and resonance Raman spectroscopies, force field simulations, and density functional theory calculations. Biochemistry 50 5220-5235... 

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