PMID:6297458: Difference between revisions

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<span style = 'font-size: large'> '''Cammack, R, Jackson, RH, Cornish-Bowden, A and Cole, JA'''  (1982) Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12.''Biochem. J.'' '''207''':333-9</span>
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|{{TableHeadingColor}} |'''Abstract''' || <protect>The NADH-dependent nitrite reductase of Escherichia coli, which contains sirohaem, flavin, non-haem iron and labile sulphide, was examined by low-temperature e.s.r. spectroscopy. The enzyme, stored in the presence of nitrite and ascorbate, gave the spectrum of a nitrosyl derivative, with hyperfine splitting due to the nitrosyl nitrogen. On removal of these reagents, a series of signals centred around g = 6 was observed, typical of high-spin ferric haem. Cyanide converted this into a low-spin form. On reduction of the enzyme with NADH, an axial spectrum at g = 1.92, 2.01 was observed. The temperature-dependence of this signal is indicative of a [2Fe-2S] iron-sulphur cluster. The midpoint potential of this cluster was estimated to be -230 +/- 15 mV by two independent methods. Reduction of the enzyme with dithionite yielded further signals, which are at present unidentified, at g = 2.1-2.28. No signals were observed that could be assigned to a [4Fe-4S] cluster, such as is found in other sulphite reductases and nitrite reductases that contain sirohaem.</protect>
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'''Cammack, R, Jackson, RH, Cornish-Bowden, A and Cole, JA'''  (1982) Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12. ''Biochem. J.'' '''207''':333-9
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!align=left  |Abstract
*  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6297458 PubMed]
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The NADH-dependent nitrite reductase of Escherichia coli, which contains sirohaem, flavin, non-haem iron and labile sulphide, was examined by low-temperature e.s.r. spectroscopy. The enzyme, stored in the presence of nitrite and ascorbate, gave the spectrum of a nitrosyl derivative, with hyperfine splitting due to the nitrosyl nitrogen. On removal of these reagents, a series of signals centred around g = 6 was observed, typical of high-spin ferric haem. Cyanide converted this into a low-spin form. On reduction of the enzyme with NADH, an axial spectrum at g = 1.92, 2.01 was observed. The temperature-dependence of this signal is indicative of a [2Fe-2S] iron-sulphur cluster. The midpoint potential of this cluster was estimated to be -230 +/- 15 mV by two independent methods. Reduction of the enzyme with dithionite yielded further signals, which are at present unidentified, at g = 2.1-2.28. No signals were observed that could be assigned to a [4Fe-4S] cluster, such as is found in other sulphite reductases and nitrite reductases that contain sirohaem.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6297458 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153865 PMC1153865]


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Electron Spin Resonance Spectroscopy; Escherichia coli/enzymology; Heme/analogs & derivatives; Heme/metabolism; Iron/metabolism; NADH, NADPH Oxidoreductases/metabolism; Nitrite Reductase (NAD(P)H); Nitrite Reductases/metabolism; Oxidation-Reduction; Potassium Cyanide/pharmacology; Sulfur/metabolism; Thiosulfates/pharmacology
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Latest revision as of 04:49, 15 September 2013

Citation

Cammack, R, Jackson, RH, Cornish-Bowden, A and Cole, JA (1982) Electron-spin-resonance studies of the NADH-dependent nitrite reductase from Escherichia coli K12. Biochem. J. 207:333-9

Abstract

The NADH-dependent nitrite reductase of Escherichia coli, which contains sirohaem, flavin, non-haem iron and labile sulphide, was examined by low-temperature e.s.r. spectroscopy. The enzyme, stored in the presence of nitrite and ascorbate, gave the spectrum of a nitrosyl derivative, with hyperfine splitting due to the nitrosyl nitrogen. On removal of these reagents, a series of signals centred around g = 6 was observed, typical of high-spin ferric haem. Cyanide converted this into a low-spin form. On reduction of the enzyme with NADH, an axial spectrum at g = 1.92, 2.01 was observed. The temperature-dependence of this signal is indicative of a [2Fe-2S] iron-sulphur cluster. The midpoint potential of this cluster was estimated to be -230 +/- 15 mV by two independent methods. Reduction of the enzyme with dithionite yielded further signals, which are at present unidentified, at g = 2.1-2.28. No signals were observed that could be assigned to a [4Fe-4S] cluster, such as is found in other sulphite reductases and nitrite reductases that contain sirohaem.

Links

PubMed PMC1153865

Keywords

Electron Spin Resonance Spectroscopy; Escherichia coli/enzymology; Heme/analogs & derivatives; Heme/metabolism; Iron/metabolism; NADH, NADPH Oxidoreductases/metabolism; Nitrite Reductase (NAD(P)H); Nitrite Reductases/metabolism; Oxidation-Reduction; Potassium Cyanide/pharmacology; Sulfur/metabolism; Thiosulfates/pharmacology

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