Results 241 to 250 of about 7,497 (290)

The Prokaryotic Nitrate Reductases

, 2007
This chapter reviews the structural organization and bioenergetics of the four prokaryotic NO3 reductases and the eukaryotic enzyme and explores the possible mechanisms of NO3 transport. The membrane-bound NO3- reductase with the active site facing the cytoplasm is usually a three-subunit enzyme composed of NarGHI.
Richardson, David J., Van Spanning, Rob J.M., Ferguson, Stuart J.   +2 more
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Reductive activation of nitrate reductases

Dalton Transactions, 2005
Protein film voltammetry of Paracoccus pantotrophus respiratory nitrate reductase (NarGH) and Synechococcus elongatus assimilatory nitrate reductase (NarB) shows that reductive activation of these enzymes may be required before steady state catalysis is observed.
Field, Sarah J., Thornton, Nicholas P., Anderson, Lee J., Gates, Andrew J., Reilly, Ann, Jepson, Brian J. N., Richardson, David J., George, Simon J., Cheesman, Myles R., Butt, Julea N.   +9 more
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Evolution of the soluble nitrate reductase: defining the monomeric periplasmic nitrate reductase subgroup

Biochemical Society Transactions, 2006
Bacterial nitrate reductases can be classified into at least three groups according to their localization and function, namely membrane-bound (NAR) or periplasmic (NAP) respiratory and cytoplasmic assimilatory (NAS) enzymes. Monomeric NASs are the simplest of the soluble nitrate reductases, although heterodimeric NASs exist, and a common structural ...
Jepson, B. J. N., Marietou, A., Mohan, S., Cole, J. A., Butler, C. S., Richardson, D. J.   +5 more
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Bacterial nitrate reductases: Molecular and biological aspects of nitrate reduction [PDF]

Journal of Inorganic Biochemistry, 2006
Nitrogen is a vital component in living organisms as it participates in the making of essential biomolecules such as proteins, nucleic acids, etc. In the biosphere, nitrogen cycles between the oxidation states +V and -III producing many species that ...
JOSÉ J G Moura, CARLOS D Brondino
exaly   +2 more sources

Functional domains of assimilatory nitrate reductases and nitrite reductases

Trends in Biochemical Sciences, 1990
Biochemical investigation of nitrate assimilation enzymes spans the past four decades. With the molecular cloning of genes for nitrate reductases and nitrite reductases, exciting new prospects are developing for the study of these enzymes.
Wilbur H Campbell, James R Kinghorn
exaly   +2 more sources

Molybdenum-free nitrate reductases from vanadate-reducing bacteria

FEBS Letters, 1998
Two catalytically distinct molybdenum-free dissimilatory nitrate reductases, a soluble periplasmic and a membrane-bound one, were isolated from the vanadate-reducing facultatively anaerobic bacterium Pseudomonas isachenkovii and purified to ...
Alexey N Antipov, Tatiana V Khijniak, N P L'Vov   +2 more
exaly   +2 more sources

Functional, biochemical and genetic diversity of prokaryotic nitrate reductases

Cellular and Molecular Life Sciences, 2001
Prokaryotic nitrate reduction can serve a number of physiological roles and can be catalysed by a number of biochemically distinct nitrate reductases. Three distinct nitrate reductase classes can be indentified in prokaryotes, NAS, NAR and NAP.
Ben C Berks, Stephen Spiro, David J Richardson   +2 more
exaly   +2 more sources

Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5å resolution: relationship to other flavoprotein reductases

Structure, 1994
Background In the biological assimilation of nitrate in plants and microorganisms, nitrate is reduced to ammonium by transfer of eight electrons in a two-step process.
Guoguang Lu, Wilbur H Campbell, Ylva Lindqvist   +2 more
exaly   +2 more sources

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Regulation of Nitrate Reductase in Chlorella. Nitrate Requirement for the Appearance of Nitrate Reductase Activity

Plant Science Letters, 1983
Summary Cells of Chlorella vulgaris (Cambridge culture collection, strain 211/12) grown in chemostat under conditions of nitrate limitation, exhibit very high levels of nitrate reductase activity. Similar levels of activity were found in cells grown in chemostat with a limited nitrogen source constituted by 75% ammonium plus 25% nitrate. By contrast,
Di Martino Rigano V, Vona V, FUGGI, Amodio, Di Martino C, Rigano C.   +4 more
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Nitrate reductase and cytochrome bnitrate reductase structural genes as parts of the nitrate reductase operon

Molecular and General Genetics MGG, 1981
The existence of a nitrate-reductase operon in the tryptophane region was deduced from the effects of prophage insertion in each of chlI and chlC genes and from transposition of the Mu-mediated host DNA fragments of F-prime. This operon appears to be polarized from chlC to chlI and the gene order in the region is trp -- chlI -- chlC -- purB.
V, Bonnefoy-Orth, M, Lepelletier, M C, Pascal, M, Chippaux   +3 more
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