The two-haem nitrite reductase of Micrococcus denitrificans

Newton, N. A.

doi:10.1016/0005-2744(69)90425-2

Cited by 140 publications

(30 citation statements)

References 22 publications

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“…The molecular weight of the T. denitrijicans nitrite reductase was 120000, in agreement with the enzyme from M. denitriJicans (Newton, 1969) and P. aeruginosa (Gudat, Singh & Wharton, 1973). Values of 90000 and 85000 have also been reported for the P. aeruginosa enzyme (Horio et al, 1961;Newton, 1969). As for nitrite reductases from M .…”

Section: Discussionsupporting

confidence: 76%

“…The purified enzyme showed both nitrite reductase and cytochrome oxidase activities, suggesting that, as in other denitrifying bacteria, e.g. Pseudomonas aeruginosa , Microccocus denitrzjicans (Lam & Nicholas, 1969;Newton, 1969), these activities are associated with the same protein which functions with either NO2-or O2 as a terminal electron acceptor. Since in the present investigations the bacteria were grown anaerobically with nitrate, the physiological function of this enzyme was for nitrite reduction.…”

Section: Discussionmentioning

confidence: 85%

“…Nitrite reductase from P. aeruginosa (Horio et al, 1961), which was initially studied as cytochrome oxidase but was referred to later as nitrite reductase (Yamanaka & Okunuki, 1974), and those from M. denitriJicans (Lam & Nicholas, 1969;Newton, 1969) and Alcaligenes faecalis (Iwasaki & Matsubara, 1971) also contained haem c and d. In the present investigations haem c and d were shown to be in the ratio of 1 : 1 as was also reported for nitrite reductase from P. aeruginosa (Horio et al, 1961) and A. faecalis (Iwasaki & Matsubara, 1971). The molecular weight of the T. denitrijicans nitrite reductase was 120000, in agreement with the enzyme from M. denitriJicans (Newton, 1969) and P. aeruginosa (Gudat, Singh & Wharton, 1973). Values of 90000 and 85000 have also been reported for the P. aeruginosa enzyme (Horio et al, 1961;Newton, 1969).…”

Section: Discussionmentioning

confidence: 99%

“…denitrijicans and P . aeruginosa have also been reported to serve as electron donors for nitrite reduction and cytochrome oxidase (Horio et al, 1961;Newton, 1969).…”

Section: Discussionmentioning

confidence: 99%

“…A crystal of K,Fe(CN), was added to the reference cuvette to oxidize the green haem. The AA618-650 between the reference and sample cuvettes was determined on a double-beam recording spectrophotometer and the amount of green haem was calculated using the absorption coefficient of 19.6 mM-l cm-l (Newton, 1969).…”

Section: Introductionmentioning

confidence: 99%

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Sulphide-linked Nitrite Reductase from Thiobacillus denitrificans with Cytochrome Oxidase Activity: Purification and Properties

Sawhney

Nicholas

1978

Journal of General Microbiology

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A membrane-bound, sulphide-linked nitrite reductase from Thiobacillus denitrz3cans was solubilized and after further purification its properties were examined. The purified enzyme, mol. wt 120000, contained cytochromes c and din the ratio of 1 : 1. Both cytochromes were reduced by sulphide and re-oxidized with nitrite or air. Oxidation by nitrite resulted in the appearance of an absorption peak at 572 nm. The kinetics of the reduction of the enzyme with sulphide indicated that cytochrome c was reduced before cytochrome d. The redox potential of cytochrome d was 22 mV more positive than that of cytochrome c. Cytochromes c and d were dissociated from the purified enzyme by treatment with sodium dodecyl sulphate. The purified nitrite reductase also had cytochrome oxidase activity and both the activities were stimulated by cytochrome c-55 1 isolated from T. denitriJicans. Reduced cytochrome c-551 was an effective electron donor for the purified enzyme with either nitrite or air as the terminal electron acceptor. Neither cytochrome c-554 (also isolated from T. denitrzjicans) nor mammalian cytochrome c was effective as reductant for the enzyme. NO and N 2 0 were identified as the products of nitrite reduction by the purified sulphidelinked nitrite reductase.

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Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

“…denitrijicans and P . aeruginosa have also been reported to serve as electron donors for nitrite reduction and cytochrome oxidase (Horio et al, 1961;Newton, 1969).…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Sulphide-linked Nitrite Reductase from Thiobacillus denitrificans with Cytochrome Oxidase Activity: Purification and Properties

Sawhney

Nicholas

1978

Journal of General Microbiology

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Hemes, Chlorophylls, and Related Compounds: Biosynthesis and Metabolic Regulation

Granick¹,

Beale²

1978

Advances in Enzymology - And Related Areas of Molecular Biology

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Formation of a potent respiratory inhibitor at nitrite reduction by nitrite reductase isolated from the bacterium Paracoccus denitrificans

Kučera¹,

Skládal²

1990

J. Basic Microbiol.

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A new method of dissimilatory nitrite reductase (cytochrome cd1) isolation from the periplasmic fraction of anaerobically grown cells of the bacterium Paracoccus denitrificans was developed, using ionex and gel permeation chromatography with FPLC system (Pharmacia, Sweden). In experiments with isolated enzyme it was shown that through a nitrite reduction, catalysed by this enzyme, a substance (presumably nitric oxide) was formed which at submicromolar concentrations inhibited terminal cytochrome oxidase of the respiratory chain of the same bacterium. These results help to explain formerly observed sensitivity of bacterial oxidase activity to NO2- and the mechanism of switching the electron flow from O2 to nitrogen terminal acceptors.

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The two-haem nitrite reductase of Micrococcus denitrificans

Cited by 140 publications

References 22 publications

Sulphide-linked Nitrite Reductase from Thiobacillus denitrificans with Cytochrome Oxidase Activity: Purification and Properties

Sulphide-linked Nitrite Reductase from Thiobacillus denitrificans with Cytochrome Oxidase Activity: Purification and Properties

Hemes, Chlorophylls, and Related Compounds: Biosynthesis and Metabolic Regulation

Formation of a potent respiratory inhibitor at nitrite reduction by nitrite reductase isolated from the bacterium Paracoccus denitrificans

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