HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Conover, R. C. Articles by Johnson, M. K. Search for Related Content PubMed PubMed Citation Articles by Conover, R. C. Articles by Johnson, M. K. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 15, 8533-8541, 05, 1990

Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin

RC Conover, AT Kowal, WG Fu, JB Park, S Aono, MW Adams and MK Johnson
School of Chemical Sciences, University of Georgia, Athens 30602.

Pyrococcus furiosus ferredoxin is the only known example of a ferredoxin containing a single [4Fe-4S] cluster that has non-cysteinyl ligation of one iron atom, as evidenced by the replacement of a ligating cysteine residue by an aspartic acid residue in the amino acid sequence. The properties of the iron-sulfur cluster in both the aerobically and anaerobically isolated ferredoxin have been characterized by EPR, magnetic circular dichroism, and resonance Raman spectroscopies. The anaerobically isolated ferrodoxin contains a [4Fe- 4S]+,2+ cluster with anomalous properties in both the oxidized and reduced states which are attributed to aspartate and/or hydroxide coordination of a specific iron atom. In the reduced form, the cluster exists with a spin mixture of S = 1/2 (20%) and S = 3/2 (80%) ground states. The dominant S = 3/2 form has a unique EPR spectrum that can be rationalized by an S = 3/2 spin Hamiltonian with E/D = 0.22 and D = +3.3 +/- 0.2 cm-1. The oxidized cluster has an S = 0 ground state, and the resonance Raman spectrum is characteristic of a [4Fe-4S]2+ cluster except for the unusually high frequency for the totally symmetric breathing mode of the [4Fe-4S] core, 342 cm-1. Comparison with Raman spectra of other [4Fe-4S]2+ centers suggests that this behavior is diagnostic of anomalous coordination of a specific iron atom. The iron- sulfur cluster is shown to undergo facile and quantitative [4Fe-4S] in equilibrium [3Fe-4S] interconversion, and the oxidized and reduced forms of the [3Fe-4S] cluster have S = 1/2 and S = 2 ground states, respectively. In both redox states the [3Fe-4S]0,+ cluster exhibits spectroscopic properties analogous to those of similar clusters in other bacterial ferredoxins, suggesting non-cysteinyl coordination for the iron atom that is removed by ferricyanide oxidation. Aerobic isolation induces partial degradation of the [4Fe-4S] cluster to yield [3Fe-4S] and possibly [2Fe-2S] centers. Evidence is presented to show that only the [4Fe-4S] form of this ferredoxin exists in vivo.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				G. Shen, R. Balasubramanian, T. Wang, Y. Wu, L. M. Hoffart, C. Krebs, D. A. Bryant, and J. H. Golbeck SufR Coordinates Two [4Fe-4S]2+, 1+ Clusters and Functions as a Transcriptional Repressor of the sufBCDS Operon and an Autoregulator of sufR in Cyanobacteria J. Biol. Chem., November 2, 2007; 282(44): 31909 - 31919. [Abstract] [Full Text] [PDF]

				X. Brazzolotto, J. K. Rubach, J. Gaillard, S. Gambarelli, M. Atta, and M. Fontecave The [Fe-Fe]-Hydrogenase Maturation Protein HydF from Thermotoga maritima Is a GTPase with an Iron-Sulfur Cluster J. Biol. Chem., January 13, 2006; 281(2): 769 - 774. [Abstract] [Full Text] [PDF]

				P. Hanzelmann, H. L. Hernandez, C. Menzel, R. Garcia-Serres, B. H. Huynh, M. K. Johnson, R. R. Mendel, and H. Schindelin Characterization of MOCS1A, an Oxygen-sensitive Iron-Sulfur Protein Involved in Human Molybdenum Cofactor Biosynthesis J. Biol. Chem., August 13, 2004; 279(33): 34721 - 34732. [Abstract] [Full Text] [PDF]

				L. Grgic, K. Zwicker, N. Kashani-Poor, S. Kerscher, and U. Brandt Functional Significance of Conserved Histidines and Arginines in the 49-kDa Subunit of Mitochondrial Complex I J. Biol. Chem., May 14, 2004; 279(20): 21193 - 21199. [Abstract] [Full Text] [PDF]

				F. Pierrel, H. L. Hernandez, M. K. Johnson, M. Fontecave, and M. Atta MiaB Protein from Thermotoga maritima: CHARACTERIZATION OF AN EXTREMELY THERMOPHILIC tRNA-METHYLTHIOTRANSFERASE J. Biol. Chem., August 8, 2003; 278(32): 29515 - 29524. [Abstract] [Full Text] [PDF]

				K.-S. Yoon, C. Bobst, C. F. Hemann, R. Hille, and F. R. Tabita Spectroscopic and Functional Properties of Novel 2[4Fe-4S] Cluster-containing Ferredoxins from the Green Sulfur Bacterium Chlorobium tepidum J. Biol. Chem., November 16, 2001; 276(47): 44027 - 44036. [Abstract] [Full Text] [PDF]

				A. Liu and A. Graslund Electron Paramagnetic Resonance Evidence for a Novel Interconversion of [3Fe-4S]+ and [4Fe-4S]+ Clusters with Endogenous Iron and Sulfide in Anaerobic Ribonucleotide Reductase Activase in Vitro J. Biol. Chem., April 21, 2000; 275(17): 12367 - 12373. [Abstract] [Full Text] [PDF]

				H. S. Gao-Sheridan, M. A. Kemper, R. Khayat, G. J. Tilley, F. A. Armstrong, V. Sridhar, G. S. Prasad, C. D. Stout, and B. K. Burgess A T14C Variant of Azotobacter vinelandii Ferredoxin I Undergoes Facile [3Fe-4S]0 to [4Fe-4S]2+ Conversion in Vitro but Not in Vivo J. Biol. Chem., December 11, 1998; 273(50): 33692 - 33701. [Abstract] [Full Text] [PDF]

				Y.-S. Jung, I. R. Vassiliev, J. Yu, L. McIntosh, and J. H. Golbeck Strains of Synechocystis sp. PCC 6803with Altered PsaC. II. EPR AND OPTICAL SPECTROSCOPIC PROPERTIES OF FA AND FB IN ASPARTATE, SERINE, AND ALANINE REPLACEMENTS OF CYSTEINES 14and 51 J. Biol. Chem., March 21, 1997; 272(12): 8040 - 8049. [Abstract] [Full Text] [PDF]

				T. Yano, S. S. Chu, V. D. Sled', T. Ohnishi, and T. Yagi The Proton-translocating NADH-Quinone Oxidoreductase (NDH-1) of Thermophilic Bacterium Thermus thermophilus HB-8. COMPLETE DNA SEQUENCE OF THE GENE CLUSTER AND THERMOSTABLE PROPERTIES OF THE EXPRESSED NQO2 SUBUNIT J. Biol. Chem., February 14, 1997; 272(7): 4201 - 4211. [Abstract] [Full Text] [PDF]

				Y.-S. Jung, I. R. Vassiliev, F. Qiao, F. Yang, D. A. Bryant, and J. H. Golbeck Modified Ligands to FA and FB in Photosystem I. PROPOSED CHEMICAL RESCUE OF A [4Fe-4S] CLUSTER WITH AN EXTERNAL THIOLATE IN ALANINE, GLYCINE, AND SERINE MUTANTS OF PsaC J. Biol. Chem., December 6, 1996; 271(49): 31135 - 31144. [Abstract] [Full Text] [PDF]

				T. Mehari, F. Qiao, M. P. Scott, D. F. Nellis, J. Zhao, D. A. Bryant, and J. H. Golbeck Modified Ligands to F(A) and F(B) in Photosystem I J. Biol. Chem., November 24, 1995; 270(47): 28108 - 28117. [Abstract] [Full Text] [PDF]

				Y.-S. Jung, C. A. Bonagura, G. J. Tilley, H. S. Gao-Sheridan, F. A. Armstrong, C. D. Stout, and B. K. Burgess Structure of C42D Azotobacter vinelandii FdI. A Cys-X-X-Asp-X-X-Cys MOTIF LIGATES AN AIR-STABLE [4Fe-4S]2+/+ CLUSTER J. Biol. Chem., November 17, 2000; 275(47): 36974 - 36983. [Abstract] [Full Text] [PDF]

				T. Iwasaki, E. Watanabe, D. Ohmori, T. Imai, A. Urushiyama, M. Akiyama, Y. Hayashi-Iwasaki, N. J. Cosper, and R. A. Scott Spectroscopic Investigation of Selective Cluster Conversion of Archaeal Zinc-containing Ferredoxin from Sulfolobus sp. Strain 7 J. Biol. Chem., August 11, 2000; 275(33): 25391 - 25401. [Abstract] [Full Text] [PDF]