Literature DB >> 2997176

The high potential iron-sulfur center in Escherichia coli fumarate reductase is a three-iron cluster.

J E Morningstar, M K Johnson, G Cecchini, B A Ackrell, E B Kearney.   

Abstract

The fumarate reductase complex and soluble enzyme from Escherichia coli have been investigated by low temperature magnetic circular dichroism and electron paramagnetic resonance spectroscopies. The results confirm the presence of one [2Fe-2S] cluster and show that the high potential iron-sulfur center is a 3Fe cluster of the type found in bacterial ferredoxins. Since the 3Fe cluster is present in catalytically competent enzyme and does not appear to be involved in any type of cluster conversion under reducing conditions, we conclude that it is an intrinsic component of the functional enzyme. The significance of the results is discussed in relation to the published amino acid sequence and the iron-sulfur cluster composition of bacterial fumarate reductases.

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Year:  1985        PMID： 2997176

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  11 in total

Review 1.  The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.

Authors:  Behrooz Moosavi; Edward A Berry; Xiao-Lei Zhu; Wen-Chao Yang; Guang-Fu Yang
Journal:  Cell Mol Life Sci       Date:  2019-06-24       Impact factor: 9.261

2.  Perturbation of the quinone-binding site of complex II alters the electronic properties of the proximal [3Fe-4S] iron-sulfur cluster.

Authors:  Jonathan Ruprecht; So Iwata; Richard A Rothery; Joel H Weiner; Elena Maklashina; Gary Cecchini
Journal:  J Biol Chem       Date:  2011-02-10       Impact factor: 5.157

3.  Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster.

Authors:  M T Werth; G Cecchini; A Manodori; B A Ackrell; I Schröder; R P Gunsalus; M K Johnson
Journal:  Proc Natl Acad Sci U S A       Date:  1990-11       Impact factor: 11.205

4.  The succinate dehydrogenase from the thermohalophilic bacterium Rhodothermus marinus: redox-Bohr effect on heme bL.

Authors:  A S Fernandes; M M Pereira; M Teixeira
Journal:  J Bioenerg Biomembr       Date:  2001-08       Impact factor: 2.945

5.  Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide.

Authors:  G Cecchini; C R Thompson; B A Ackrell; D J Westenberg; N Dean; R P Gunsalus
Journal:  Proc Natl Acad Sci U S A       Date:  1986-12       Impact factor: 11.205

6.  Iron-sulfur protein maturation in Helicobacter pylori: identifying a Nfu-type cluster carrier protein and its iron-sulfur protein targets.

Authors:  Stéphane L Benoit; Ashley A Holland; Michael K Johnson; Robert J Maier
Journal:  Mol Microbiol       Date:  2018-03-30       Impact factor: 3.501

7.  Nucleotide sequence encoding the flavoprotein and iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex.

Authors:  M K Phillips; L Hederstedt; S Hasnain; L Rutberg; J R Guest
Journal:  J Bacteriol       Date:  1987-02       Impact factor: 3.490

8.  The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli.

Authors:  U Wissenbach; A Kröger; G Unden
Journal:  Arch Microbiol       Date:  1990       Impact factor: 2.552

9.  A conserved lysine residue controls iron-sulfur cluster redox chemistry in Escherichia coli fumarate reductase.

Authors:  Victor W T Cheng; Quang M Tran; Nasim Boroumand; Richard A Rothery; Elena Maklashina; Gary Cecchini; Joel H Weiner
Journal:  Biochim Biophys Acta       Date:  2013-05-24

10.  Regulation of Escherichia coli fumarate reductase (frdABCD) operon expression by respiratory electron acceptors and the fnr gene product.

Authors:  H M Jones; R P Gunsalus
Journal:  J Bacteriol       Date:  1987-07       Impact factor: 3.490
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