Endonuclease III is an iron-sulfur protein

Cunningham, Richard P.; Asahara, Hitomi; Bank, Janet F.; Scholes, Charles P.; Salerno, John C.; Surerus, Kristene K.; Münck, Eckard; McCracken, John; Peisach, Jack; Emptage, Mark H.

doi:10.1021/bi00436a049

Cited by 221 publications

(213 citation statements)

References 42 publications

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“…Previous investigations of Endo III with EPR spectroscopy at 10K after exposure to ferricyanide revealed a signal attributed to the [3Fe-4S] 1+ cluster [8]. A cationic oxidant, Co(phen) 3 3+ (phen = 1,10-phenanthroline), that binds DNA, was employed to determine whether binding of the protein to DNA might promote oxidation of the [4Fe-4S] 2+ cluster in solution [56].…”

Section: Epr Studies With Co(phen) 3 3+ As An Oxidant In Solutionmentioning

confidence: 99%

“…Many BER glycosylases contain a [4Fe-4S] cluster [8][9][10], the function of which is unknown. Endonuclease III (Endo III) was the first glycosylase discovered to contain this metal cofactor [8].…”

Section: Introductionmentioning

confidence: 99%

“…Endonuclease III (Endo III) was the first glycosylase discovered to contain this metal cofactor [8]. Endo III removes a wide variety of oxidized pyrimidines from DNA and contains the helixhairpin-helix (HhH) recognition motif [11][12][13][14][15][16][17][18][19].…”

Section: Introductionmentioning

confidence: 99%

“…Earlier, experiments were performed with Endo III to determine the properties and function of the [4Fe-4S] cluster [8,35]. Mossbauer and electron paramagnetic resonance (EPR) spectroscopy experiments confirmed that the protein contains the [4Fe-4S] 2+ cluster when the protein is not bound to DNA.…”

Section: Introductionmentioning

confidence: 99%

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DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

Boal

Yavin

Barton

2007

Journal of Inorganic Biochemistry

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The [4Fe-4S] cluster is ubiquitous to a class of base excision repair enzymes, in organisms ranging from bacteria to man, and was first considered as a structural element, owing to its redox stability under physiological conditions. When studied bound to DNA, two of these repair proteins (MutY and Endonuclease III from Escherichia coli) display DNA-dependent reversible electron transfer with characteristics typical of high potential iron proteins. These results have inspired a reexamination of the role of the [4Fe-4S] cluster in this class of enzymes. Might the [4Fe-4S] cluster be used as a redox cofactor to search for damaged sites using DNA-mediated charge transport, a process well known to be highly sensitive to lesions and mismatched bases? Described here are experiments demonstrating the utility of DNA-mediated charge transport in characterizing these DNA-binding metalloproteins, as well as efforts to elucidate this new function for DNA as an electronic signaling medium among the proteins.

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Section: Epr Studies With Co(phen) 3 3+ As An Oxidant In Solutionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

Boal

Yavin

Barton

2007

Journal of Inorganic Biochemistry

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“…The existence of different types of [Fe-S] proteins and clusters points to a remarkable functional and structural diversity, reflecting the chemical versatility of both iron and sulfur [3,4]. The known functions of biological [Fe-S] clusters include electron transfer in Fds and redox enzymes [1,[5][6][7], coupled electron/proton transfer [8], substrate binding and activation [9][10][11][12][13][14][15][16][17][18][19], Fe or cluster storage [20], structural control [21][22][23], regulation of gene expression [24][25][26][27][28][29][30][31] and enzyme activity [32][33][34], disulfide reduction [35][36][37] and sulfur donation [38][39][40].…”

Section: Introductionmentioning

confidence: 99%

Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster

et al. 2006

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Desulfovibrio gigas ferredoxin II (DgFdII) is a small protein with a polypeptide chain composed of 58 amino acids, containing one Fe 3 S 4 cluster per monomer. Upon studying the redox cycle of this protein, we detected a stable intermediate (FdII int ) with four 1 H resonances at 24.1, 20.5, 20.8 and 13.7 ppm. The differences between FdII ox and FdII int were attributed to conformational changes resulting from the breaking/formation of an internal disulfide bridge. The same 1 H NMR methodology used to fully assign the three cysteinyl ligands of the [3Fe-4S] core in the oxidized state (DgFdII ox ) was used here for the assignment of the same three ligands in the intermediate state (DgFdII int ). The spin-coupling model used for the oxidized form of DgFdII where magnetic exchange coupling constants of around 300 cm À1 and hyperfine coupling constants equal to 1 MHz for all the three iron centres were found, does not explain the isotropic shift temperature dependence for the three cysteinyl cluster ligands in DgFdII int . This study, together with the spin delocalization mechanism proposed here for DgFdII int , allows the detection of structural modifications at the [3Fe-4S] cluster in DgFdII ox and DgFdII int .

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Iron–Sulfur Proteins

Johnson

Smith

2005

Encyclopedia of Inorganic Chemistry

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Iron–sulfur proteins contain iron coordinated by at least one sulfur ligand and include proteins with mononuclear Fe centers with partial or complete cysteinyl sulfur ligation as well as proteins containing clusters of iron and inorganic sulfide. This review summarizes the structural, electronic, and redox properties of protein‐bound mononuclear FeS centers and FeS clusters containing [2Fe2S], [3Fe4S], and [4Fe4S] cores. In addition to the ubiquitous role in mediating biological electron transport, the roles of FeS centers have proliferated to include coupling of electron and proton transfer, substrate binding and activation, determining protein structure, regulation of gene expression and enzymatic activity, disulfide reduction, and iron, electron, or cluster storage. The diverse roles of FeS clusters are illustrated by discussion of specific systems: the mitochondrial and photosynthetic electron transport chains and a wide range of soluble redox enzymes and proteins; the active sites of nitrile hydratase, aconitase‐type (de)hydratases, superoxide reductase (SOR), radical‐SAM (S‐adenosylmethionine) enzymes, NiFe‐ and Fe‐hydrogenase, sulfite and nitrite reductase, nitrogenase, CO dehydrogenase, and acetyl‐CoA synthase; the structural FeS centers in DNA repair enzymes; the regulatory roles of FeS centers in the SoxR, fumarate–nitrate reduction (FNR), IscR/SufR, and iron‐regulatory protein (IRP) proteins and in selected enzymes; the two classes of FeS cluster containing disulfide reductases typified by ferredoxin–thioredoxin reductase (FTR) and heterodisulfide reductase (HDR); and the role of 8Fe ferredoxins and polyferredoxins in iron, electron, or cluster storage.

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Endonuclease III is an iron-sulfur protein

Cited by 221 publications

References 42 publications

DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

DNA repair glycosylases with a [4Fe–4S] cluster: A redox cofactor for DNA-mediated charge transport?

Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster

Iron–Sulfur Proteins

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