Overproduction of the prismane protein from Desulfovibrio desulfuricans ATCC 27774 in Desulfovibrio vulgaris (Hildenborough) and EPR spectroscopy of the [6Fe-6S] cluster in different redox states

Berg, W.A.M. van den; Stevens, A.A.M.; Verhagen, M.J.F.M.; Dongen, W.M.A.M. van; Hagen, W.R.

doi:10.1016/0167-4838(94)90214-3

Cited by 31 publications

(28 citation statements)

References 23 publications

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“…Its up-regulation in the presence of nitrite and nitrate suggests that HCP is involved in nitrite or nitrate reduction. Being a redox-active protein, based on the structural and spectroscopic studies [3,10,11], HCP appears to accomplish an as yet unidentified reaction in the nitrogen cycle. To investigate this possibility HCP has been overexpressed from a recombinant plasmid for physiological studies.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional regulation of a hybrid cluster (prismane) protein

Filenko

Browning

Cole

2005

Biochemical Society Transactions

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HCP (hybrid-cluster protein) contains two Fe/S clusters, one of which is a hybrid [4Fe-2S-2O] cluster. Despite intensive study, its physiological function has not been reported. The Escherichia coli hcp gene is located in a two-gene operon with hcr, which encodes an NADH-dependent HCP reductase. E. coli HCP is detected after anaerobic growth with nitrate or nitrite: possible roles for it in hydroxylamine or nitric oxide reduction have been proposed. To study the regulation and role of HCP, an hcp::lacZ fusion was constructed and transformed into fnr, arcA and norR mutant strains of E. coli. Transcription from the hcp promoter was induced during anaerobic growth. Only the fnr mutant was defective in hcp expression. Nitrate- and nitrite-induced transcription from the hcp promoter was activated by the response regulator proteins NarL and NarP. Gel retardation assays were used to show that FNR (fumarate-nitrate regulation) and NarL form a complex with the hcp promoter. Transcription of the hcp-hcr operon initiates at a thymine nucleotide located 31 bp upstream of the translation-initiation codon. HCP has been overexpressed from a recombinant plasmid for physiological studies.

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Section: Discussionmentioning

confidence: 99%

Transcriptional regulation of a hybrid cluster (prismane) protein

Filenko

Browning

Cole

2005

Biochemical Society Transactions

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“…Spectroscopic, sequence data, and X-ray structural evidence points to the possibility of similar 'superclusters' in other ironsulfur redox enzymes, viz sulfite reductase [25], CO dehydrogenase [26,27], and nitrogenase [28,29]. This information combined with what is known on the redox properties of small, electron transfer iron-sulfur proteins [4] has led us to hypothesize the following seniority scheme for the redox properties of biological iron-sulfur clusters [30][31][32].…”

Section: Discussionmentioning

confidence: 99%

Electrochemical study of the redox properties of [2Fe‐2S] ferredoxins Evidence for superreduction of the Rieske [2Fe‐2S] cluster

Verhagen¹,

Link²,

Hagen³

1995

FEBS Letters

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what determines the reduction potential(s) of these proteins, and what determines whether their functioning is associated with the transfer of no, one, one pair, or multiple pairs of electrons.By a fortunate coincidence of circumstances we have found it possible to study the complete redox behaviour of a biological [2Fe-2S] system: (i) the Rieske protein can be purified as a water-soluble fragment with no observable change in its ironsulfur cluster [5]; (ii) the fragment exhibits a direct, unmediated electrochemical response on glassy carbon [6]; (iii) the first reduction potential of the Rieske cluster is unusually high, namely Era,7 = + 0.3 V [7]; (iv) carbon electrodes have a high overpotential for H 2 evolution, therefore, their use allows for aqueous-solution bio-electrochemistry down to E = -1 V [8]. The voltammetric characterization of the Rieske cluster and the comparison of its properties with other (i.e. low-potential) biological [2Fe-2S] clusters are the subject of this study.

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“…The dithionite-reduced protein exhibits resonances around g = 5.3 and 4.5, characteristic of an S = 312 spin system, as well as the S = 1/2 prismane-like spectrum. Both the prismane proteins from D. vulgaris 191 and D. desulfuricans [7] have been cloned and overexpressed in D. vulgaris.The crystallographic structure for the prismane protein is not yet determined though a novel, possibly [6Fe-6S], cluster is implicated from the EPR characteristics. Analysis of the protein as isolated and the reduced protein by Mossbauer spectroscopy suggests that the cluster consists of four iron atoms of delocal-…”

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confidence: 99%

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confidence: 99%

“…The dithionite-reduced protein exhibits resonances around g = 5.3 and 4.5, characteristic of an S = 312 spin system, as well as the S = 1/2 prismane-like spectrum. Both the prismane proteins from D. vulgaris 191 and D. desulfuricans [7] ized electronic nature and two charge-localized irons, possibly coordinated by nitrogen [4]. Possible cluster binding regions can be identified in the primary structure of the protein from comparison of the D. desul-,furicans and D. vulgaris nucleotide sequences [6].…”

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confidence: 99%

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Characterization of the Prismane Protein from Desulfovibrio vulgaris (Hildenborough) by Low‐Temperature Magnetic Circular Dichroic Spectroscopy

Marritt

Farrar

Bretón

et al. 1995

European Journal of Biochemistry

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The prismane protein of Desulfovibrio vulgaris (Hildenborough) contains a putative cluster.This novel iron-sulfur cluster has been characterized here by magnetic circular dichroism (MCD) spectroscopy. Three paramagnetic redox states of the cluster, , each show a distinctive low-temperature MCD spectrum which is unlike that observed for any other iron-sulfur clusters. Magnetization data for the prismane protein in these three redox states indicate ground state spins that are in accordance with previous EPR assignments. For and 5 141. The S = 112 signal is unusual for an iron-sulfur cluster in having g-values all below 2.00, these are 1.971, 1.951 and 1.898. The low-field part of the spectrum shows resonances at around g = 15 and a complex spectrum between g = 9.7 and g = 5.2, these have been correlated to an S = 912 spin system A prismane protein has also been identified in D. desulfuricans and shows similar but not identical spectroscopic properties [6-81. This protein, as isolated, has a spin state that is almost completely S = 9/2, with only 3% S = 1/2 spinslmolecule. The dithionite-reduced protein exhibits resonances around g = 5.3 and 4.5, characteristic of an S = 312 spin system, as well as the S = 1/2 prismane-like spectrum. Both the prismane proteins from D. vulgaris 191 and D. desulfuricans [7] have been cloned and overexpressed in D. vulgaris.The crystallographic structure for the prismane protein is not yet determined though a novel, possibly [6Fe-6S], cluster is implicated from the EPR characteristics. Analysis of the protein as isolated and the reduced protein by Mossbauer spectroscopy suggests that the cluster consists of four iron atoms of delocal-

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Overproduction of the prismane protein from Desulfovibrio desulfuricans ATCC 27774 in Desulfovibrio vulgaris (Hildenborough) and EPR spectroscopy of the [6Fe-6S] cluster in different redox states

Cited by 31 publications

References 23 publications

Transcriptional regulation of a hybrid cluster (prismane) protein

Transcriptional regulation of a hybrid cluster (prismane) protein

Electrochemical study of the redox properties of [2Fe‐2S] ferredoxins Evidence for superreduction of the Rieske [2Fe‐2S] cluster

Characterization of the Prismane Protein from Desulfovibrio vulgaris (Hildenborough) by Low‐Temperature Magnetic Circular Dichroic Spectroscopy

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