scholarly journals Purification of NADPH dehydrogenase from a hyperthemophile, Pyrobaculum islandicum

2009 ◽  
Vol 8 (1) ◽  
pp. 31-35
Author(s):  
M Tanigawa ◽  
S Seki ◽  
M Mohri ◽  
A Harigae ◽  
Y Nagata
Keyword(s):  
Pyrobaculum Islandicum ◽  
Nadph Dehydrogenase

scholarly journals An Arabidopsis Mutant with High Cyclic Electron Flow around Photosystem I (hcef) Involving the NADPH Dehydrogenase Complex

2010 ◽  
Vol 22 (1) ◽  
pp. 221-233 ◽  
Author(s):  
Aaron K. Livingston ◽  
Jeffrey A. Cruz ◽  
Kaori Kohzuma ◽  
Amit Dhingra ◽  
David M. Kramer
Keyword(s):  
Photosystem I ◽  
Electron Flow ◽  
Cyclic Electron Flow ◽  
Arabidopsis Mutant ◽  
Nadph Dehydrogenase ◽  
Dehydrogenase Complex

Enzymological Characteristics of the Hyperthermostable NAD-Dependent Glutamate Dehydrogenase from the Archaeon Pyrobaculum islandicum and Effects of Denaturants and Organic Solvents

1998 ◽  
Vol 64 (6) ◽  
pp. 2152-2157 ◽  
Author(s):  
Chizu Kujo ◽  
Toshihisa Ohshima
Keyword(s):  
Enzyme Activity ◽  
Glutamate Dehydrogenase ◽  
Organic Solvents ◽  
Crude Extract ◽  
Guanidine Hydrochloride ◽  
Hyperthermophilic Enzyme ◽  
Hyperthermophilic Archaeon ◽  
Spectrum Change ◽  
Molecular Masses ◽  
Pyrobaculum Islandicum

ABSTRACT NAD-dependent glutamate dehydrogenase (l-glutamate:NAD oxidoreductase, deaminating; EC 1.4.1.2 ) was purified to homogeneity from a crude extract of the continental hyperthermophilic archaeonPyrobaculum islandicum by two successive Red Sepharose CL-4B affinity chromatographies. The enzyme is the most thermostable NAD-dependent dehydrogenase found to date; the activity was not lost after incubation at 100°C for 2 h. The enzyme activity increased linearly with temperature, and the maximum was observed at ca. 90°C. The enzyme has a molecular mass of about 220 kDa and consists of six subunits with identical molecular masses of 36 kDa. The enzyme required NAD as a coenzyme for l-glutamate deamination and was different from the NADP-dependent glutamate dehydrogenase from other hyperthermophiles. The Km values for NAD,l-glutamate, NADH, 2-oxoglutarate, and ammonia were 0.025, 0.17, 0.0050, 0.066, and 9.7 mM, respectively. The enzyme activity was significantly increased by the addition of denaturants such as guanidine hydrochloride and some water-miscible organic solvents such as acetonitrile and tetrahydrofuran. When fluorescence of the enzyme was measured in the presence of guanidine hydrochloride, a significant emission spectrum change and a shift in the maximum were observed but not in the presence of urea. These results indicate that this hyperthermophilic enzyme may have great potential in applications to biosensor and bioreactor processes.

scholarly journals Constraints on Anaerobic Respiration in the Hyperthermophilic Archaea Pyrobaculum islandicum and Pyrobaculum aerophilum

2007 ◽  
Vol 74 (2) ◽  
pp. 396-402 ◽  
Author(s):  
Lawrence F. Feinberg ◽  
R. Srikanth ◽  
Richard W. Vachet ◽  
James F. Holden
Keyword(s):  
Iron Oxide ◽  
Growth Rates ◽  
Direct Contact ◽  
Iron Reduction ◽  
Elemental Sulfur ◽  
Reductase Activity ◽  
Anaerobic Respiration ◽  
Hyperthermophilic Archaea ◽  
Pyrobaculum Aerophilum ◽  
Pyrobaculum Islandicum

ABSTRACT Pyrobaculum islandicum uses iron, thiosulfate, and elemental sulfur for anaerobic respiration, while Pyrobaculum aerophilum uses iron and nitrate; however, the constraints on these processes and their physiological mechanisms for iron and sulfur reduction are not well understood. Growth rates on sulfur compounds are highest at pH 5 to 6 and highly reduced (<−420-mV) conditions, while growth rates on nitrate and iron are highest at pH 7 to 9 and more-oxidized (>−210-mV) conditions. Growth on iron expands the known pH range of growth for both organisms. P. islandicum differs from P. aerophilum in that it requires direct contact with insoluble iron oxide for growth, it did not produce any extracellular compounds when grown on insoluble iron, and it lacked 2,6-anthrahydroquinone disulfonate oxidase activity. Furthermore, iron reduction in P. islandicum appears to be completely independent of c-type cytochromes. Like that in P. aerophilum, NADH-dependent ferric reductase activity in P. islandicum increased significantly in iron-grown cultures relative to that in non-iron-grown cultures. Proteomic analyses showed that there were significant increases in the amounts of a putative membrane-bound thiosulfate reductase in P. islandicum cultures grown on thiosulfate relative to those in cultures grown on iron and elemental sulfur. This is the first evidence of this enzyme being used in either a hyperthermophile or an archaeon. Pyrobaculum arsenaticum and Pyrobaculum calidifontis also grew on Fe(III) citrate and insoluble iron oxide, but only P. arsenaticum could grow on insoluble iron without direct contact.

scholarly journals NdhP Is an Exclusive Subunit of Large Complex of NADPH Dehydrogenase Essential to Stabilize the Complex inSynechocystissp. Strain PCC 6803

2014 ◽  
Vol 289 (27) ◽  
pp. 18770-18781 ◽  
Author(s):  
Jingsong Zhang ◽  
Fudan Gao ◽  
Jiaohong Zhao ◽  
Teruo Ogawa ◽  
Quanxi Wang ◽  
...  
Keyword(s):  
Large Complex ◽  
Nadph Dehydrogenase ◽  
Pcc 6803

scholarly journals Identification and Characterization of UDP-Glucose Dehydrogenase from the Hyperthermophilic Archaon,Pyrobaculum islandicum

2011 ◽  
Vol 75 (10) ◽  
pp. 2049-2051 ◽  
Author(s):  
Takenori SATOMURA ◽  
Kaori KUSUMI ◽  
Toshihisa OHSHIMA ◽  
Haruhiko SAKURABA
Keyword(s):  
Glucose Dehydrogenase ◽  
Pyrobaculum Islandicum ◽  
Identification And Characterization
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