Enzymatic Properties and Effect of Ionic Strength on Periplasmic Nitrate Reductase (NAP) fromDesulfovibrio desulfuricansATCC 27774

1997 ◽  
Vol 239 (3) ◽  
pp. 816-822 ◽  
Author(s):  
S.A. Bursakov ◽  
C. Carneiro ◽  
M.J. Almendra ◽  
R.O. Duarte ◽  
J. Caldeira ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Nitrate Reductase ◽  
Enzymatic Properties ◽  
Periplasmic Nitrate Reductase

The periplasmic nitrate reductase of

1993 ◽  
Vol 51 (1-2) ◽  
pp. 369
Author(s):  
B.C. Berks ◽  
D.J. Richardson ◽  
S. Marritt ◽  
A.J. Thomson ◽  
S.J. Ferguson
Keyword(s):  
Nitrate Reductase ◽  
Periplasmic Nitrate Reductase

Oxygen control of nitrogen oxide respiration, focusing on α-proteobacteria

2011 ◽  
Vol 39 (1) ◽  
pp. 179-183 ◽  
Author(s):  
James P. Shapleigh
Keyword(s):  
Nitrate Reductase ◽  
Nitrogen Oxide ◽  
Physiological Function ◽  
Physiological Role ◽  
Present Review ◽  
Oxygen Control ◽  
Anoxic Conditions ◽  
Periplasmic Nitrate Reductase

Denitrification is generally considered to occur under micro-oxic or anoxic conditions. With this in mind, the physiological function and regulation of several steps in the denitrification of model α-proteobacteria are compared in the present review. Expression of the periplasmic nitrate reductase is quite variable, with this enzyme being maximally expressed under oxic conditions in some bacteria, but under micro-oxic conditions in others. Expression of nitrite and NO reductases in most denitrifiers is more tightly controlled, with expression only occurring under micro-oxic conditions. A possible exception to this may be Roseobacter denitrificans, but the physiological role of these enzymes under oxic conditions is uncertain.

scholarly journals Compensatory periplasmic nitrate reductase activity supports anaerobic growth ofPseudomonas aeruginosaPAO1 in the absence of membrane nitrate reductase

2009 ◽  
Vol 55 (10) ◽  
pp. 1133-1144 ◽  
Author(s):  
Nadine E. Van Alst ◽  
Lani A. Sherrill ◽  
Barbara H. Iglewski ◽  
Constantine G. Haidaris
Keyword(s):  
Nitrate Reductase ◽  
Response Regulator ◽  
Reductase Activity ◽  
Transcriptional Start Site ◽  
Atp Synthesis ◽  
Anaerobic Growth ◽  
Start Site ◽  
Terminal Electron Acceptor ◽  
Periplasmic Nitrate Reductase ◽  
Growth Recovery

Nitrate serves as a terminal electron acceptor under anaerobic conditions in Pseudomonas aeruginosa . Reduction of nitrate to nitrite generates a transmembrane proton motive force allowing ATP synthesis and anaerobic growth. The inner membrane-bound nitrate reductase NarGHI is encoded within the narK1K2GHJI operon, and the periplasmic nitrate reductase NapAB is encoded within the napEFDABC operon. The roles of the 2 dissimilatory nitrate reductases in anaerobic growth, and the regulation of their expressions, were examined by use of a set of deletion mutants in P. aeruginosa PAO1. NarGHI mutants were unable to grow anaerobically, but plate cultures remained viable up to 120 h. In contrast, the nitrate sensor-response regulator mutant ΔnarXL displayed growth arrest initially, but resumed growth after 72 h and reached the early stationary phase in liquid culture after 120 h. Genetic, transcriptional, and biochemical studies demonstrated that anaerobic growth recovery by the NarXL mutant was the result of NapAB periplasmic nitrate reductase expression. A novel transcriptional start site for napEFDABC expression was identified in the NarXL mutant grown anaerobically. Furthermore, mutagenesis of a consensus NarL-binding site monomer upstream of the novel transcriptional start site restored anaerobic growth recovery in the NarXL mutant. The data suggest that during anaerobic growth of wild-type P. aeruginosa PAO1, the nitrate response regulator NarL directly represses expression of periplasmic nitrate reductase, while inducing maximal expression of membrane nitrate reductase.

scholarly journals NapF Is a Cytoplasmic Iron-Sulfur Protein Required for Fe-S Cluster Assembly in the Periplasmic Nitrate Reductase

2004 ◽  
Vol 279 (48) ◽  
pp. 49727-49735 ◽  
Author(s):  
M. Francisca Olmo-Mira ◽  
Mónica Gavira ◽  
David J. Richardson ◽  
Francisco Castillo ◽  
Conrado Moreno-Vivián ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Cluster Assembly ◽  
Periplasmic Nitrate Reductase ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

THROMBIN PROPERTIES

1957 ◽  
Vol 35 (1) ◽  
pp. 743-758 ◽  
Author(s):  
Edward Ronwin
Keyword(s):  
Ionic Strength ◽  
Substrate Specificity ◽  
Enzymatic Activity ◽  
Enzymatic Properties ◽  
Organic Reagents

The enzymatic properties of thrombin have been examined and compared with those of two related enzymes, plasmin and trypsin. The effects of factors such as pH, substrate specificity, ionic strength, cations, anions, and organic reagents on the enzymatic activity of thrombin have been studied. While the three enzymes discussed possess differences, such similarities as were observed are quite striking and permit their classification into one group as tryptic enzymes.

The nitrate-sensing NasST system regulates nitrous oxide reductase and periplasmic nitrate reductase inBradyrhizobium japonicum

2014 ◽  
Vol 16 (10) ◽  
pp. 3263-3274 ◽  
Author(s):  
Cristina Sánchez ◽  
Manabu Itakura ◽  
Takashi Okubo ◽  
Takashi Matsumoto ◽  
Hirofumi Yoshikawa ◽  
...  
Keyword(s):  
Nitrous Oxide ◽  
Nitrate Reductase ◽  
Nitrous Oxide Reductase ◽  
Periplasmic Nitrate Reductase

scholarly journals Novel growth characteristics and high rates of nitrate reduction of anEscherichia colistrain, LCB2048, that expresses only a periplasmic nitrate reductase

2000 ◽  
Vol 185 (1) ◽  
pp. 51-57 ◽  
Author(s):  
Laura C. Potter ◽  
Paul D. Millington ◽  
Gavin H. Thomas ◽  
Richard A. Rothery ◽  
Gérard Giordano ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Growth Characteristics ◽  
Periplasmic Nitrate Reductase
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