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. 2002 Dec;11(12):2969-73.
doi: 10.1110/ps.0222402.

Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters

Nathaniel J Cosper  1 , D Matthew Eby, Asako Kounosu, Norio Kurosawa, Ellen L Neidle, Donald M Kurtz Jr, Toshio Iwasaki, Robert A Scott
Affiliations

Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters

Nathaniel J Cosper et al. Protein Sci. 2002 Dec.

Abstract

Proteins containing Rieske-type [2Fe-2S] clusters play important roles in many biological electron transfer reactions. Typically, [2Fe-2S] clusters are not directly involved in the catalytic transformation of substrate, but rather supply electrons to the active site. We report herein X-ray absorption spectroscopic (XAS) data that directly demonstrate an average increase in the iron-histidine bond length of at least 0.1 A upon reduction of two distantly related Rieske-type clusters in archaeal Rieske ferredoxin from Sulfolobus solfataricus strain P-1 and bacterial anthranilate dioxygenases from Acinetobacter sp. strain ADP1. This localized redox-dependent structural change may fine tune the protein-protein interaction (in the case of ARF) or the interdomain interaction (in AntDO) to facilitate rapid electron transfer between a lower potential Rieske-type cluster and its redox partners, thereby regulating overall oxygenase reactions in the cells.

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Figures

Fig. 1.
Fig. 1.
EXAFS (top) and sulfur phase-corrected Fourier transforms (bottom, over k = 2–13.5 Å−1) of oxidized (a) and reduced (b) ARF (solid) and AntDO (dashed). The vertical line in the Fourier transform is positioned to illustrate the shift to longer distance of the shoulder of the first shell peak, which represents the Fe-Nimid scattering shell. X-ray absorption Fe K edge spectra (bottom, inset) for oxidized (a) and reduced (b) ARF (solid) and AntDO (dashed).
Fig. 2.
Fig. 2.
Comparison of the goodness-of-fit value (f`) with the Fe-Nimid bond distance for oxidized (dashed) and reduced (solid) ARF (open circles) and AntDO (filled circles) in fits where the Fe-Nimid distance was constrained to the specified value and the Fe-Nimid Debye-Waller factor was constrained to be 0.0020 Å2. Lines connect the points for visual comparison.
See this image and copyright information in PMC

References

    1. Berry, E.A., Guergova-Kuras, M., Huang, L.-S., and Crofts, A.R. 2000. Structure and function of cytochrome bc complexes. Annu. Rev. Biochem. 69 1005–1075. - PubMed
    1. Brugna, M., Nitschke, W., Asso, M., Guigliarelli, B., Lemesle-Meunier, D., and Schmidt, C. 1999. Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms. J. Biol. Chem. 274 16766–16772. - PubMed
    1. Carrell, C.J., Zhang, H., Cramer, W.A., and Smith, J.L. 1997. Biological identity and diversity in photosynthesis and respiration: Structure of the lumen-side domain of the chloroplast Rieske protein. Structure 5 1613–1625. - PubMed
    1. Cline, J.F., Hoffman, B.M., Mims, W.B., LaHaie, E., Ballou, D.P., and Fee, J.A. 1985. Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas. J. Biol. Chem. 260 3251–3254. - PubMed
    1. Colbert, C.L., Couture, M.M.-J., Eltis, L.D., and Bolin, J. 2000. A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8 1267–1278. - PubMed

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