Results 261 to 270 of about 251,937 (291)
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Further Characterization of Nitrate and Nitrite Reductases from Chlamydomonas reinhardii

, 1976
The enzymes responsible for nitrate reduction in Chlamydomonas reinhardii, namely NADH-nitrate reductase and ferredoxin-nitrite reductase, have been further characterized.
J. Barea, J. Maldonado, J. Cárdenas
semanticscholar   +1 more source

NO Production by Pseudomonas aeruginosa cd1 Nitrite Reductase [PDF]

open access: possibleIUBMB Life, 2003
AbstractThe structural and catalytic properties of Pseudomonas aeruginosa cd1 nitrite reductase, a key enzyme in bacterial denitrification, are reviewed in this paper. The mechanism of reduction of nitrite to NO is discussed in detail with special attention to the structural interpretation of function.
CUTRUZZOLA', Francesca   +3 more
openaire   +2 more sources

Electron transport through nitrate and nitrite reductases in Campylobacter jejuni.

Biochemical Society Transactions, 2005
Campylobacter jejuni is a small genome pathogen that is incapable of growing strictly anaerobically due to its dependence on an oxygen-requiring ribonucleotide reductase for DNA synthesis.
M. S. Pittman, D. Kelly
semanticscholar   +1 more source

The induction of nitrite reductase in Neurospora crassa

Biochimica et Biophysica Acta (BBA) - General Subjects, 1972
Abstract Like nitrate reductase, nitrite reductase in Neurospora crassa is induced by either nitrate of nitrite and is repressed by ammonia. None of the enzymatic activities associated with the nitrite reductase, i.e. NADPH-nitrite reductase, reduced benzyl viologen-nitrite reductase or NADPH-hydroxylamine reductase, were derepressible when ...
openaire   +3 more sources

Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 A resolution: comparison of blue and green nitrite reductases.

Journal of Biochemistry (Tokyo), 1998
The crystal structure of the blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 (AxgNIR) has been determined at 2.05 A resolution. AxgNIR contains both type 1 and 2 Cu sites, the geometry of the former being distorted tetrahedral.
T. Inoue   +8 more
semanticscholar   +1 more source

Bidirectional Catalysis by Copper-Containing Nitrite Reductase

Biochemistry, 2004
The copper-containing nitrite reductase from Alcaligenes faecalis S-6 was found to catalyze the oxidation of nitric oxide to nitrite, the reverse of its physiological reaction. Thermodynamic and kinetic constants with the physiological electron donor pseudoazurin were determined for both directions of the catalyzed reaction in the pH range of 6-8.
Wijma, H.J.   +3 more
openaire   +4 more sources

Magnetization of the sulfite and nitrite complexes of oxidized sulfite and nitrite reductases: EPR silent spin S = 1/2 states.

Biochemistry, 1988
The saturation magnetizations of the sulfite complex of oxidized sulfite reductase and the nitrite complex of oxidized nitrite reductase have been measured to determine their spin state.
Edmund P. Day   +5 more
semanticscholar   +1 more source

DFT Study on Nitrite Reduction Mechanism in Copper-Containing Nitrite Reductase

Biochemistry, 2015
Dissimilatory reduction of nitrite by copper-containing nitrite reductase (CuNiR) is an important step in the geobiochemical nitrogen cycle. The proposed mechanisms for the reduction of nitrite by CuNiRs include intramolecular electron and proton transfers, and these two events are understood to couple.
Juha M. Lintuluoto, Masami Lintuluoto
openaire   +3 more sources

A novel enzyme electrode method for the determination of nitrite based on nitrite reductase

Analytica Chimica Acta, 1975
The enzyme, nitrite reductase, can be extracted and purified from spinach leaves; the freeze-dried preparation is completely stable for at least 4 months if kept in a freezer. The enzyme catalyzes the reduction of nitrite to ammonia in the presence of reduced methyl viologen as electron donor.
Chih-Hen. Kiang   +2 more
openaire   +3 more sources

nitrite reductases

Catalysis from A to Z, 2020
C. Wong
semanticscholar   +1 more source

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